# Patent

## Title
MEK1 polypeptides

## Abstract

The present invention provides, inter alia, crystals of the MEK1 polypeptide which are particularly useful for structure based drug design as well as methods of use thereof.

## Background
This application claims the benefit of U.S. provisional patent application No. 60/800,876; filed May 16, 2006; which is herein incorporated by reference in its entirety.


FIELD OF THE INVENTION
The present invention relates, inter alga, to crystals comprising MEK1 polypeptide and methods of use thereof.
BACKGROUND OF THE INVENTION
The protein kinases that constitute mitogen activated protein kinase (MAPK) pathways are of interest for their central role in mediating cellular responses to stimuli such as growth factors and cytokines. The MAPK kinase, MEK1, is activated by a phosphorylation signaling cascade in response to hormones and growth factors. Known oncogenes such as Ras and Raf are upstream activators of MEK1 and MEK1 is aberrantly activated in multiple common tumor types. Inhibition of MEK1 reverses cellular transformation. Hence, there is considerable interest in the role MEK1 signaling plays in oncogenic transformation and in targeting MEK1 for cancer therapies using, for example, small molecules. Structure assisted drug design is a tool used to optimize the success of identifying such therapeutic compounds. However, use of this powerful methodology requires three-dimensional structural information (e.g., as obtained via X-ray diffraction of the target protein). The crystal structures of unphosphorylated MEK1 have been reported, by Chen et al., in a ternary complex with ATP and 5-bromo-N-(2,3-dihydroxyl-propoxy)-3,4-difluoro-2(2-fluoro-4-iodo-phenylamino)-benzamide or {5-[3,4-difluoro-2-(2-fluoro-4-iodo-phenylamino)-phenyl]-1,3,4-oxadiazol-2-yl}-(2-morpholin-4-yl-ethyl)-amine (“Chen crystal”; see EP1321518A1; WO 2003/54180 or U.S. 2003/0224500). This crystals suffers from several drawbacks. For example, the ATP and the benzamide compound in the MEK1 crystal disclosed by Chen at al.




(Cpd.3)) is extremely difficult to displace, e.g., by soaking, with another compound. The Chen crystal is likely not soakabie because cpd.3 is an allosteric compound that makes a complex network of interactions with both the MEK1 protein and any nucleotide bound to MEK1. The inhibitor in the Chen crystal binds to MEK1, along with a nucleotide, with particularly high affinity making its replacement with any other compound, by soaking, impractical. This shortcoming limits the utility of this Chen crystal in identifying new therapeutically useful MEK1 inhibitors. Moreover, the crystal disclosed by Chen of al. comprises a large N-terminal deletion. The deleted region comprises an α-helical region important to the negative regulation of MEK1. The crystal structures revealed in the crystals of the present invention indicate that the region deleted in the Chen crystal is an integral part of MEK1. The deleted negative-regulatory domain makes the biological accuracy and relevance of any structural data obtained from the crystal less certain.

There remains a need in the art for crystals of MEK1 into which various inhibitors can be soaked for the purpose of evaluating the inhibitor as well as obtaining structural data for the purpose of performing structure-based drug design.
SUMMARY OF THE INVENTION
The present invention addresses the need for high quality crystals for studying complexes between MEK1 and any other inhibitor of MEK1. The crystals of the present invention comprise MEK1 complexed with compound 2 or ATPγS. The MEK1 complex crystals of the present invention, unlike the crystals presently in the art (e.g., Chen crystals), are very amenable to soaking wherein new complexes between MEK1 and a different MEK1 inhibitor (ATP competitive, non-competitive or uncompetitive) can be formed, studied and evaluated.
The inhibitors and, thus, the crystalline complexes of the present invention are also superior (e.g., to the Chen crystals) due to the fact that they bind to the MEK1 hinge region (discussed below). Since the hinge region is the region to which ATP binds, the inhibitors of the present invention (e.g., compound 2) are ATP competitive. The hinge region is characterized by its relatively high resistance to mutation and is distinct from the MEK1 binding pocket to which the inhibitors in the Chen crystal bind. Since the hinge region exhibits a low mutation frequency, the MEK1 enzyme is less likely to develop resistance to inhibitors that bind the hinge region. This characteristic, in turn, makes inhibitors identifiable using the compositions and methods of the present invention very effective anti-cancer treatments because tumors being treated with the inhibitors are unlikely to develop resistance. Additional hinge region binding inhibitors can be identified (in addition to compound 2) by computer assisted modeling techniques of the present invention or by soaking a candidate inhibitor into a crystal of the present invention and, subsequently, determining the crystalline complex structure.
Furthermore, the crystals of the present invention comprise the N-terminal negative regulatory domain discussed above, thus making structural data obtained from the present crystals more biologically relevant (see e.g., Mansour et al. Science 265:966-970 (1994)). As mentioned above, structural data from the crystals of the present invention reveal that this region is an integral part of the MEK1 structure. The region exhibits extended surface interactions with the rest of the protein.
The present invention provides an isolated polypeptide comprising amino acids 35-383 or 35-393 of human MEK1 optionally comprising mutations at 5298, S299 and Y300 e.g., S298N, S299K and Y300F. In an embodiment of the invention, the polypeptide comprises amino acids 25-373 of SEQ ID NO: 2, amino acids 25-383 of SEQ ID NO: 1 or the amino acid sequence of SEQ ID NO: 1 or 2. In an embodiment of the invention, the polypeptide is complexed with




or ATPγS or any combination thereof. In an embodiment of the invention, the polypeptide comprises a binding pocket whose three-dimensional orientation is characterized by the structural coordinates of amino acids 70-84; 93-98; 117-120; 128-129; 140-152; 193-197 and 205-208 according to Table 2, 3 or 4 wherein one or more of said binding pocket amino acids can be conservatively substituted and/or a hinge region whose three-dimensional orientation is characterized by the structural coordinates of amino acids E144, H145 and M146 according to Table 1 or amino acids E143, H144 and M145 according to Table 2, 3 or 4 wherein one or more of said hinge region amino acids can be conservatively substituted. in an embodiment of the invention, the polypeptide comprises amino acids whose three dimensional orientation is characterized by the structural coordinates of Table 1, 2, 3 or 4. In an embodiment of the invention, the polypeptide is crystalline. The present invention also comprises any polypeptide herein in a crystallizable composition. For example, in an embodiment of the invention, the crystallizable composition comprises a MEK1 polypeptide (e.g., 19.2 mg/ml concentration) of the invention, a precipitant (e.g., PEG4000 e.g., at a concentration of about 18%), a buffer (e.g., TRIS e.g., at a concentration of about 90 mM) and about 1% to about 15%, (e.g., 3%) dimethylsulfoxide (DMSO) and optionally Ca2+ (e.g., CaCl2 e.g., at a concentration of about 0.18M). In an embodiment of the invention, the crystallizable composition is at a temperature of about 4° C. In an embodiment of the invention, the polypeptide is fused to a heterologous protein. The present invention also comprise an isolated polynucleotide encoding any polypeptide set forth herein along with an isolated vector thereof or an isolated host cell comprising said vector.

The present invention also comprises a crystalline composition comprising a MEK1 binding pocket characterized by the structural coordinates of amino acid 70-84; 93-98; 117-120; 128-129; 140-152; 193-197 and 205-208 according to Table 2, 3 or 4 wherein one or more of said binding pocket amino acids can be conservatively substituted and/or a hinge region whose three-dimensional orientation is characterized by the structural coordinates of amino acids E144, H145 and M146 according to Table 1 or amino acids E143, H144 and M145 according to Table 2, 3 or 4 wherein one or more of said hinge region amino acids can be conservatively substituted. In an embodiment of the invention, the polypeptide is complexed with ATPγS and/or




The present invention also provides a crystalline composition of comprising a complex wherein the complex three dimensional structure is characterized by structural coordinates comprising a root mean square deviation of common residue backbone atoms or alpha carbon atoms of less than about 1.5 Å when superimposed on backbone atoms or alpha carbon atoms described by structural coordinates of any of Tables 1, 2, 3 or 4. In an embodiment of the invention, the polypeptide comprises the amino acid sequence of SEQ ID NO: 2 complexed with ATPγS or a compound represented by structural formula 2





which is characterized by structural coordinates set forth in Table 3 or 4. In an embodiment of the invention, the crystal comprises comprising unit cell dimensions of a=about 76.8 Å, b=about 76.8 Å, c=about 222.4 Å, a=13=about 90°; γ=about 120°; unit cell dimensions of a=about 77.2 Å, b=about 77.2 Å, c=about 222.2 Å, α=β=about 90° γ=about 120°; belongs to space group P 61 2 2; diffracts X-rays to a resolution of about 2.55 Å or a lower number; or diffracts X-rays to a resolution of about 2.45 Å or a lower number. In an embodiment of the invention, the crystalline composition comprises a polypeptide complex defined by the structural coordinates set forth in any of Tables 1-4. In an embodiment of the invention, the crystalline composition comprises an isolated polypeptide comprising amino acids 35-383 of MEK1 (e.g., 25-373 of SEQ ID NO: 2) complexed with ATPγS or





The present invention also provides a compound, an enantiomer, stereoisomer, rotamer or tautomer thereof, or a pharmaceutically acceptable salt or solvate thereof, said compound having the structure shown in Formula 2:




or a pharmaceutical composition thereof comprising a pharmaceutically acceptable carrier.
The present invention also provides a hanging-drop/sitting drop vapor diffusion method for making a crystal comprising a MEK1 polypeptide of the invention complexed with ATPγS or with compound 2 or both comprising incubating an aqueous solution comprising said polypeptide, DMSO (e.g., about 1.5% DMSO) and a precipitant (PEG4000 e.g., about 9% PEG4000) in close proximity to a precipitant solution comprising the precipitant (e.g., about 18% PEG4000) and DMSO (e.g., about 1% to about 15%, for example, about 3% DMSO) in a sealed chamber. In an embodiment of the invention, the solution comprising the polypeptide comprises a lower concentration of precipitant and the precipitant solution comprises the approximate final concentration of precipitant which the solution comprising the polypeptide will reach during incubation. In an embodiment of the invention, the polypeptide is at a concentration of about 9.6 mg/ml. In an embodiment of the invention, the precipitant solution comprises about 90 mM TRIS, pH 8.5, about 18% PEG 4000, about 0.18 M calcium chloride and about 3% DMSO. In an embodiment of the invention, the incubation occurs for about 5 to about 7 days (e.g., at 4° C.).
The present invention also provides a method for making a crystal comprising amino acids 35-373 of human MEK1 polypeptide (e.g., amino acids 25-373 of SEQ ID NO: 2) complexed with a compound represented by structural formula 2:




comprising soaking a crystal comprising said polypeptide complexed with ATPγS, with said compound. In an embodiment of the invention, about 0.1 μl of a 100 mM solution of said compound is combined with a drop of a solution comprising said crystal comprising said polypeptide complexed with ATPγS.

The present invention also provides a method for evaluating the potential of a candidate MEK1 inhibitor to associate with MEK1 comprising soaking the crystalline composition which comprises an isolated polypeptide comprising amino acids 35-373 of MEK1 complexed with ATP′S or with




with the candidate MEK1 inhibitor to form a complex between said polypeptide and said candidate and determining the three-dimensional structure of said complex.

The present invention also provides a method for making a crystalline complex between an ATP competitive inhibitor and a polypeptide comprising amino acids 35-383 of MEK1 comprising soaking a crystalline composition comprising a MEK1/N35/NKF/Cdel383-cpd2 complex wherein the complex three dimensional structure is characterized by structural coordinates comprising a root mean square deviation of common residue backbone atoms or alpha carbon atoms of less than about 1.5 Å when superimposed on backbone atoms or alpha carbon atoms described by structural coordinates of Table 3 or 4 with the ATP competitive inhibitor.
The present invention also provides a method for evaluating the potential of a candidate MEK1 inhibitor to associate with: a) a polypeptide or complex thereof wherein said polypeptide comprises a binding pocket defined by structural coordinates of MEK1/N35/NKF/Cdel383 amino acids 70-84; 93-98; 117-120; 128-129; 140-152; 193-197 and 205-208 according to Table 2, 3 or 4 wherein one or more of said binding pocket amino acids can be conservatively substituted and/or a hinge region whose three-dimensional orientation is characterized by the structural coordinates of amino acids E144, H145 and M146 according to Table 1 or amino acids E143, H144 and M145 according to Table 2, 3 or 4 wherein one or more of said hinge region amino acids can be conservatively substituted; or b) a homologue of said polypeptide of complex thereof, wherein said homologue comprises a binding pocket or hinge region comprising a three dimensional structure characterized by structural coordinates comprising a root mean square deviation of common residue backbone atoms or alpha carbon atoms of less than about 1.5 Å when superimposed on backbone atoms or alpha carbon atoms of said binding pocket or hinge region described by structural coordinates of Table 1, 2, 3 or 4 comprising the steps of: (i) employing computational means to perform a fitting operation between the candidate and the binding pocket or hinge region of the molecule or molecular complex; and (ii) analyzing the results of said fitting operation to quantify the association between the candidate and the binding pocket or hinge region; optionally, further comprising making a crystalline composition comprising said complex and determining the three-dimensional structure of said complex; optionally, further comprising modifying said candidate inhibitor and repeating said method. In an embodiment of the invention, any atom of said candidate located within 3.5 Å of any of said hinge region amino acids in said fitting operation is considered to interact with the hinge region (e.g., by hydrophobic contact or by polar interaction). In an embodiment of the invention, said crystalline composition is made by soaking a crystalline composition comprising said polypeptide complexed with ATPγS or with a compound represented by structural formula 2




with said candidate inhibitor. In an embodiment of the invention, said structural coordinates according to Table 3 or 4 describe a complex in a crystalline composition comprising unit cell dimensions of a=about 77.2 Å, b=about 77.2 Å, c=about 222.2 Å, α=β=about 90° γ=about 120°; said structural coordinates according to Table 3 or 4 describe a complex in a crystalline composition comprising unit cell dimensions of a=about 76.8 Å, b=about 76.8 Å, c=about 222.4 Å, α=β=about 90°; γ=about 120°; said structural coordinates according to Table 3 or 4 describe a complex in a crystalline composition which belongs to space group P 61 2 2; said structural coordinates according to Table 3 or 4 describe a complex in a crystalline composition which diffracts X-rays to a resolution of about 2.55 Å or a lower number; or said structural coordinates according to Table 3 or 4 describe a complex in a crystalline composition which diffracts X-rays to a resolution of about 2.45 Å or a lower number.

The present invention also provides a method for treating or preventing cancer, in a patient, comprising administering a therapeutically effective amount of a compound represented by structural formula 2 in association with a pharmaceutically acceptable composition thereof to said patient.
The present invention provides a method of utilizing molecular replacement to obtain structural information about a molecule or a molecular complex of unknown structure comprising: crystallizing said molecule or molecular complex; generating an X-ray diffraction pattern from said crystallized molecule or molecular complex; and applying at least a portion of the structural coordinates set forth in Table 1, 2, 3 or 4, or a related set of structural coordinates having a root mean square deviation of not more than about 1.5 Å away from the amino acid backbone atoms or only alpha carbon atoms of said coordinates as set forth in Table 1, 2, 3 or 4, to the X-ray diffraction pattern to generate a three-dimensional electron density map of at least a portion of the molecule or molecular complex whose structure is unknown.
The present invention further provides a method for making a crystal comprising a polypeptide comprising amino acids 35-383 of human MEK1 polypeptide (e.g., amino acids 24-373 of SEQ ID NO: 2) complexed with a candidate inhibitor of MEK1 comprising soaking a crystal comprising amino acids 35-383 of human MEK1 polypeptide complexed with a compound represented by structural formula 2:




or complexed with ATPγS with said candidate; optionally further comprising determining the three-dimensional structural coordinates of the atoms in said crystal e.g., by X-ray diffraction analysis.




BRIEF DESCRIPTION OF THE FIGURES
FIG. 1. Photomicrograph of MEK1 N35 NKF ternary complex crystals.
FIG. 2. Photomicrograph of MEK1 N35 NKF Cdel 383 ternary complex crystals.
FIG. 3. Photomicrograph of MEK1 N35 NKF Cdel 383 binary complex crystals.



DETAILED DESCRIPTION OF THE INVENTION
“Compound 1” or “cpd.1” is represented by the following structural formula:




“Compound 2” or “pd.2” is represented by the following structural formula:




ATPγS is represented by the following structural formula:




(Adenosine-5′-(3-thiotriphosphate); Adenosine 5′-O-(3-thiotriphosphate)).

Human MEK1 is a well known polypeptide and polynucleotide. There are several examples of MEK1 known in the art. See for example, the following accession numbers: Q02750 (UniProtKB/Swiss-Prot); NP—002746.1 (RefSeq peptide); L05624 (EMBL); IPI00219604.2 (IPI); AAA36318.1 (protein_id); NM—002755.2 (RefSeq DNA); and ENSG00000169032 (Ensembl Gene ID). An example of a MEK1 polypeptide amino acid sequence is as follows:








(SEQ ID NO: 12)



  1  mpkkkptpiq lnpapdgsav ngtssaetnl ealqkkleel eldeqqrkrl eafltqkqkv



 


 61  gelkdddfek iselgagngg vvfkvshkps glvmarklih leikpairnq iirelqvlhe


 


121  cnspyivgfy gafysdgeis icmehmdggs ldqvlkkagr ipeqilgkvs iavikgltyl


 


181  rekhkimhrd vkpsnilvns rgeiklcdfg vsgqlidsma nsfvgtrsym sperlqgthy


 


241  svqsdiwsmg lslvemavgr ypipppdake lelmfgcqve gdaaetpprp rtpgrplssy


 


301  gmdsrppmai felldyivne pppklpsgvf slefqdfvnk cliknpaera dlkqlmvhaf


 


361  ikrsdaeevd fagwlcstig lnqpstptha agv






The MEK1 hinge region amino acids are underscored.

In an embodiment of the invention, MEK1/N35/NKF comprises the following amino acid sequence:








(SEQ ID NO: 1)



  1  MGYYHHHHHH DYDIPTTENL YFQGKKLEEL ELDEQQRKRL EAFLTQKQKV GELKDDDFEK   60



 


 61  ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY  120


 


121  GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD  180


 


181  VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG  240


 


241  LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLNKF GMDSRPPMAI  300


 


301  FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF IKRSDAEEVD  360


 


361  FAGWLCSTIG LNQPSTPTHA AGV






The MEK1/N35/NKF polypeptide comprises a His6 tag in the first 10 residues (HHHHHH) (SEQ ID NO: 14). The underlined sequence indicates the portion of the sequence that is MEK1 sequence (residues 35-393 of MEK1; residues 25-383 of SEQ ID NO: 1). The portion of the MEK1/N35/NKF polypeptide that was crystallized in the examples set forth below comprises amino acids 24-383 of SEQ ID NO: 1. The MEK1/N35/NKF polypeptide comprises a mutation changing SSY (MEK1 residues 298-300) to NKF; the NKF residues are in bold font.
in an embodiment of the invention MEK1/N35/NKF/Cdel383 comprises the following amino acid sequence:








(SEQ ID NO: 2)



  1  MGYYHHHHHH DYDIPTTENL YFQGKKLEEL ELDEQQRKRL EAFLTQKQKV GELKDDDFEK   60



 


 61  ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY  120


 


121  GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD  180


 


181  VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG  240


 


241  LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLNKF GMDSRPPMAI  300


 


301  FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF IKRSDAEEVD  360


 


361  FAGWLCSTIG LNQ






The MEK1/N35/NKF/Cdel383 polypeptide comprises a His6 tag in the first 10 residues (HHHHHH) (SEQ ID NO: 14). The underlined sequence indicates the portion of the sequence that is MEK1 sequence (residues 35-383 of MEK1; residues 25-373 of SEQ ID NO: 2). The portion of the MEK1/N35/NKF/Cdel383 polypeptide that was crystallized in the examples set forth below comprises amino acids 24-373 of SEQ ID NO: 2. The MEK1/N35/NKF/Cdel383 polypeptide comprises a mutation changing SSY (MEK1 residues 298-300) to NKF; the NKF residues are in bold font.
An isolated polypeptide comprising, consisting of or consisting essentially of the amino acid sequence of SEQ ID NO: 1 and 2 or any mature fragment thereof (e.g., missing residues 1-24) or any fusion thereof form part of the present invention along with any composition or crystal thereof (e.g., a crystallizable compositon).
In accordance with the present invention, there may be employed conventional molecular biology, microbiology, and recombinant DNA techniques within the skill of the art. Such techniques are explained fully in the literature. See, e.g., Sambrook, Fritsch & Maniatis, Molecular Cloning: A Laboratory Manual, Second Edition (1989) Cold Spring Harbor Laboratory Press, Cold Spring. Harbor, N.Y. (herein “Sambrook et al., 1989”); DNA Cloning: A Practical Approach, Volumes I and II (D. N. Glover ed. 1985); Oligonucleotide Synthesis (M. J. Gait ed. 1984); Nucleic Acid Hybridization [B. D. Hames & S. J. Higgins eds. (1985)]; Transcription And Translation [B. D. Hames & S. J. Higgins, eds. (1984)]; Animal Cell Culture [R. I. Freshney, ed. (1986)]; Immobilized Cells And Enzymes [IRL Press, (1986)]; B. Perbal, A Practical Guide To Molecular Cloning (1984); F. M. Ausubel et al. (eds.), Current Protocols in Molecular Biology, John Wiley & Sons, Inc. (1996) (herein “Ausubel et al., 1996”).
The terms “express” and “expression” mean allowing or causing the information in a gene or DNA sequence to become manifest, e.g., producing a protein by activating the cellular functions involved in transcription and, optionally, translation of a corresponding gene or DNA sequence. A DNA sequence can be expressed using in vitro translation systems (e.g., rabbit reticulocyte lysate-based systems) or in or by a cell to form an “expression product” such as a mRNA or a protein. The expression product, e.g. the resulting protein, may also be referred to as “expressed”.
An insect cell used in this invention includes any cell derived from an organism of the class Insecta. In an embodiment of the invention, the insect is Spodoptera fruigiperda (Sf9 or Sf21) or Trichoplusia ni (High 5). Examples of insect expression systems that can be used with the present invention, for example to produce MEK1 polypeptides, include Bac-To-Bac (Invitrogen Corporation, Carlsbad, Calif.) or Gateway (Invitrogen Corporation, Carlsbad, Calif.).
It may also be desirable to add a heterologous protein (i.e., other than a MEK1 polypeptide of the invention) at the amino- or carboxy-terminus of a MEK1 polypeptide of the invention, e.g., to prepare a fusion protein. In one embodiment, the addition is a polyhistidine or a histidine tag comprising 12 or 18 histidines. In an embodiment of the invention, a myc tag is added to a MEK1 polypeptide of the invention. The myc tag may be used for detection or immunopurification of the MEK1. For example, the myc tag and the polyhistidine tag may both be located at the carboxy-terminus or amino-terminus in a doubly-tagged MEK1. Other heterologous proteins include, for example, GST, maltose binding protein (MBP), FLAG tag, biotin, green fluorescent protein (GFP), Strep tag (WSHPQFEK) (SEQ ID NO: 13), protein A, protein G or NusA. Detectable tags that may be fused to a MEK1 polypeptide of the invention include 32P, 35S, 3H, 99mTc, 123I, 111In, 68Ga, 18F, 125I, 131I, 113mIn, 76Br, 67Ga, 99mTc, 123I, 111In and 68Ga. Methods for constructing and using such fusions are very conventional and well known in the art.
The terms “isolated polynucleotide” or “isolated polypeptide” include a polynucleotide (e.g., RNA or DNA molecule, or a mixed polymer) or a polypeptide, respectively, which are partially or fully separated from other components that are normally found in cells or in recombinant DNA expression systems. These components include, but are not limited to, cell membranes, cell walls, ribosomes, polymerases, serum components and extraneous genomic sequences.
An isolated polynucleotide or polypeptide will, in an embodiment of the invention, be an essentially homogeneous composition of molecules.
The term “host cell” includes any cell of any organism that is selected, modified, transfected, transformed, grown, or used or manipulated in any way, for the production of a substance by the cell, for example the expression or replication, by the cell, of a gene, a DNA or RNA sequence or a protein. In an embodiment of the invention, a host cell is a bacterial cell, such as E. coli or a Chinese hamster ovary (CHO) cell.
The term “vector” includes a vehicle (e.g., a plasmid) by which a DNA or RNA sequence can be introduced into a host cell, so as to transform the host and, optionally, promote expression and/or replication of the introduced sequence.
Vectors that can be used in this invention include plasmids, viruses, bacteriophage, integratable DNA fragments, and other vehicles that may facilitate introduction of the nucleic acids into the genome of the host. Plasmids are the most commonly used form of vector but all other forms of vectors which serve a similar function and which are, or become, known in the art are suitable for use herein. See, e.g., Pouwels, at al., Cloning Vectors: A Laboratory Manual, 1985 and Supplements, Elsevier, N.Y., and Rodriguez at al. (eds.), Vectors: A Survey of Molecular Cloning Vectors and Their Uses, 1988, Buttersworth, Boston, Mass.
Prokaryotic host-vector systems include a wide variety of vectors for many different species. A representative vector for amplifying DNA is pBR322 or many of its derivatives (e.g., pUC18 or 19). Vectors that can be used to express a MEK1 polypeptide of the invention include, but are not limited to, those containing the lac promoter (pUC-series); trp promoter (pBR322-trp); Ipp promoter (the pIN-series); lambda-pP or pR promoters (pOTS); or hybrid promoters such as ptac (pDR540). See Brosius at al., “Expression Vectors Employing Lambda-, trp-, lac-, and Ipp-derived Promoters”, in Rodriguez and Denhardt (eds.) Vectors: A Survey of Molecular Cloning Vectors and Their Uses, 1988, Buttersworth, Boston, pp. 205-236. Many polypeptides can be expressed, at high levels, in an E. coli/T7 expression system as disclosed in U.S. Pat. Nos. 4,952,496, 5,693,489 and 5,869,320 and in Davanloo, P., at al., (1984) Proc. Natl. Acad. Sci. USA 81: 2035-2039; Studier, F. W., et al., (1986) J. Mol. Biol. 189: 113-130; Rosenberg, A. H., et at., (1987) Gene 56: 125-135; and Dunn, J. J., et al., (1988) Gene 68: 259.
Crystals
The present invention comprises mutant MEK1 polypeptide crystals which are complexed with ATPγS, AMP-PNP, AMP-PCP and/or a compound represented by structural formula 1 or 2. The present invention includes crystals comprising MEK1/N35/NKF complexed with ATPγS and compound 1 (MEK1/N35/NKF-ATPγS, cpd1); MEK1/N35/NKF/Cdel383 complexed with ATPγS alone (MEK1/N35/NKF/Cdel383-ATP-(S) or with ATPγS and compound 1 (MEK11N35/NKF/Cdel383-ATPγS, cpd1) as well as MEK1/N35/NKF/Cdel383 complexed with compound 2 (MEK1/N35/NKF/Cdel383-cpd2).
The present invention further comprises any crystal comprising a human MEK1 binding pocket characterized by the three dimensional configuration of amino acids 70-84; 93-98; 117-120; 128-129; 140-152; 193-197 and 205-208 in any of tables 2-4 and/or a hinge region comprising amino acids E144, H145 and M146 according to Table 1 or amino acids E143, H144 and M145 according to Table 2, 3 or 4 or a complex thereof wherein the binding pocket or hinge region is complexed with ATPγS, compound 1 or compound 2 or a combination thereof. Moreover, for the purpose of this invention, any crystalline molecule comprising a binding pocket or hinge region, optionally, complexed with ATPγS, compound 1 or compound 2 or a combination thereof, characterized by structural coordinates having a root mean square deviation (RMSD) (discussed below) of conserved residue backbone atoms (N, Cα, C, O) or of alpha carbon atoms (Cα) only of said human MEK1 binding pocket or hinge region residues of less than about 1.5 Å when superimposed—using backbone atoms or alpha carbon atoms—on the relevant binding pocket or hinge region structure coordinates of any of Tables 1-4 are considered identical and are within the scope of the present invention. In an embodiment of the invention, the crystal comprises a polypeptide comprising the amino acid sequence of SEQ ID NO: 1 or 2. In an embodiment, the root mean square deviation is about 1.0 Å or about 0.75 Å or about 0.5 Å or about 0.25 Å or about 0.10 Å.
Several crystallization methods are known in the art (Giegé, et al., (1994) Acta Crystallogr. D50: 339-350; McPherson, (1990) Eur. J. Biochem. 189: 1-23). Such methods include microbatch, hanging drop, seeding and dialysis. In an embodiment of the invention, hanging-drop vapor diffusion (McPherson, (1976) J. Biol. Chem. 251: 6300-6303) or microbatch methods (Chayen (1997) Structure 5: 1269-1274) are used. In each of these methods, it is important to promote continued crystal growth after nucleation by maintaining a supersaturated solution.
In an embodiment of the invention, in a sitting drop vapor diffusion technique, a drop composed of a mixture of MEK1 protein of the invention and precipitation reagent (e.g., PEG4000) is seated in a drop chamber in vapor equilibration with a liquid reservoir of reagent. Typically the drop contains a lower precipitation reagent concentration than the reservoir. To achieve equilibrium, water vapor leaves the drop and eventually ends up in the reservoir. As water leaves the drop, the sample undergoes an increase in relative supersaturation. Both the sample and reagent increase in concentration as water leaves the drop for the reservoir. Equilibration is reached when the reagent concentration in the drop is approximately the same as that in the reservoir. In an embodiment of the invention, the hanging drop vapor diffusion technique is essentially identical to the sitting drop vapor diffusion method, except that the protein/reagent drop is located on the underside of a surface above the reservoir. Typically the protein drops are deposited on a plate that is inverted and used as a cover over the plate containing the reservoir wells. As with sitting drop, water vapor leaves the drop and eventually ends up in the reservoir until the reagent concentration in the drop is approximately the same as that in the reservoir. In an embodiment of the invention, in the microbatch method a small drop of sample combined with the precipitation reagent of choice (e.g., PEG4000) is pipetted under a layer of paraffin oil. In a batch, or microbatch experiment, all of the reagents involved in the crystallization are present at a specific concentration and no significant concentration change of protein or reagents can occur in the drop. A modification of the microbatch under oil technique is where silicon oil is used in a mixture of 1:1 with the paraffin oil, allowing diffusion of water from the drop through the oil, hence a microbatch experiment that does allow for concentration of the sample and the reagents in the drop. In the dialysis method, polypeptide is retained in a sealed dialysis membrane which is placed into a solution containing precipitant. Equilibration across the membrane increases the precipitant concentration thereby causing the polypeptide to reach supersaturation levels. In an embodiment of the invention, it is desirable to use MEK1 preparation having a concentration of at least about 10 mg/mL, for example, 15, 20, 25 or 30 mg/mL. It may also be desirable to include a protein stabilizing agent.
Crystallization itself can be used as a purification method. In some instances, a polypeptide or protein crystallizes from a heterogeneous mixture into crystals. Isolation of such crystals by filtration and/or centrifugation, followed by redissolving the polypeptide affords a purified solution suitable for use in growing high-quality crystals which are preferred for diffraction analysis.
Once a crystal of the present invention is grown or otherwise made, X-ray diffraction data can be collected. One method for determining structure with X-ray diffraction data includes use of synchrotron radiation, under standard cryogenic condition; however, alternative methods may also be used. For example, crystals can be characterized by using X-rays produced by a conventional source, such as a sealed tube or a rotating anode. Methods of characterization include, but are not limited to, precession photography, oscillation photography and diffractometer data collection.
The crystallizable compositions provided by this invention are amenable to X-ray crystallography for providing the three-dimensional structure of MEK1 or a mutant or complex thereof. The present invention includes crystals which effectively diffract X-rays for the determination of the atomic coordinates of MEK1 or a mutant or complex thereof to a resolution of greater than about 5.0 Angstroms (e.g., about 4.5 Å, about 4.0 Å, about 3 Å, about 2.5 Å, about 2 Å, about 1.95 Å, about 1 Å), preferably greater than about 4.0 Angstroms (e.g., about 3 Å, about 2.5 Å, about 2 Å, about 1.95 Å, about 1 Å), more preferably greater than about 2.8 Angstroms (e.g., about 2.5 Å, about 2 Å, about 1.95 Å, about 1 Å) and most preferably greater than about 2.0 Angstroms (e.g., about 1.95 Å, about 1.5 Å, about 1.0 Å). in an embodiment of the invention, the resolution of a crystal of the present invention is 3.4 Å, 2.2 Å, 2.45 Å or 2.55 Å.
The present invention includes MEK1/N35/NKF-ATPγS, cpd1; MEK1/N35/NKF/Cdel383-ATPγS; MEK1/N35/NKF/Cdel383-ATPγS, cpd1 and MEK1/N35/NKF/Cdel383-cpd2 crystals whose three-dimensional structure is described by the structure coordinates set forth in Tables 1-4. The scope of the present invention also includes crystals that possess structural coordinates which are similar to those set forth in Tables 1-4. Structural similarity between crystals is discussed in detail below.
The term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a beam of X-rays by the atoms (scattering centers) of a molecule. The diffraction data are used to calculate electron density maps and to establish the positions of the individual atoms of the molecule.
The present invention includes crystals exhibiting structural coordinates which are similar to those set forth in Tables 1-4 but for crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, additions, subtractions, rotations or translations to sets of the structure coordinates or any combinations of the above. Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal may also account for variations in structure coordinates. If such variations are within an acceptable standard error as compared to the coordinates of Tables 1-4, the resulting three-dimensional shape is considered to be the same and, accordingly, the modified crystal is considered to be within the scope of the present invention.
Various computational analyses may be used to determine whether a crystal is sufficiently similar to the crystals whose structural coordinates are set forth in Tables 1-4 as to be considered the same. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.) version 4.1, and as described in the accompanying User's Guide.
The Molecular Similarity application permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure. In general, the procedure used in Molecular Similarity to compare structures is divided into four steps: 1) input the structures to be compared; 2) define the atom equivalences in these structures; 3) perform a fitting operation; and 4) analyze the results. Each structure is identified by a name. One structure is identified as the target (i.e., the fixed structure); all remaining structures are working structures (i.e., moving structures). Since atom equivalency within QUANTA is defined by user input, for the purpose of this invention we will define equivalent atoms as alpha carbon atoms (Cα) or all protein backbone atoms (N, Cα, C and O) for all conserved residues between the two structures being compared. When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses a least squares fitting algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atom is an absolute minimum. This number, given in Angströms, is reported by QUANTA.
The term “root mean square deviation” (RMSD) is a commonly known term in the art which, in general, means the square root of the arithmetic mean of the squares of the deviations from the mean distance of corresponding atoms. It is a way to express the deviation or variation from a trend or object.
The term “least squares” relates to a method based on the principle that the best estimate of a value is that in which the sum of the squares of the deviations of observed values is a minimum.
For the purpose of this invention, any crystalline molecule characterized by a set of structure coordinates that has a RMSD of conserved residue backbone atoms (N, Cα, C, O) or of alpha carbon atoms (Cα) only of less than about 1.5 Å when superimposed—using backbone atoms or alpha carbon atoms—on the relevant structure coordinates of any of Tables 1-4 are considered identical and are within the scope of the present invention. In an embodiment of the invention, the crystal comprises a polypeptide comprising the amino acid sequence of SEQ ID NO: 1 or 2. In an embodiment, the root mean square deviation is about 1.0 Å or about 0/5 Å or about 0.5 Å or about 0.25 Å or about 0.10 Å.
Computers
In accordance with the present invention, the structure coordinates of MEK1/N35/NKF-ATPγS, cpd1; MEK1/N35/NKF/Cdel383-ATPγS; MEK1/N35/NKF/Cdel383-ATPγS, cpd1 or MEK1/N35/NKF/Cdel383-cpd2 may be stored in a machine-readable storage medium. Such data may be used for a variety of purposes, such as X-ray crystallographic analysis of a protein crystal. Accordingly, one aspect of this invention provides a machine-readable data storage medium comprising a data storage material encoded with the structure coordinates set forth in Tables 1, 2, 3 or 4. The machine-readable data storage medium may also include any set of structure coordinates of a molecule that has a root mean square deviation of alpha carbon atoms (Cα) or of conserved residue backbone atoms (N, Cα, C, O) of less than about 1.5 Å, preferably, less than about 1.0 Å, more preferably less than about 0.5 Å and even more preferably less than about 0.1 Å when superimposed—using backbone atoms or only alpha carbon atoms (Cα)—on the relevant structure coordinates of Table 1-4 (discussed above).
A computer system, useful in reading the machine readable data storage medium, includes a computer comprising a central processing unit (“CPU”) and a memory storage device and is also within the scope of the present invention. In general, the computer system may be any computer with an operating system such as MS-DOS, PC-DOS, Windows, OS/2, Unix, Unix variant or MacOS. Examples of such computer systems are the Silicon Graphics Octane workstation or Compaq AlphaServer DS20. Other hardware systems and software packages will be known to those skilled in the art. Input hardware coupled to the computer system by input line, may be implemented in a variety of ways. Machine-readable data of this invention may be input via the use of a modem or modems connected by a telephone line or a dedicated data line. Alternatively or additionally, the input hardware may comprise CD-ROM drives or disk drives. A keyboard may also be used as an input device.
Output hardware, coupled to the computer system by output lines, may similarly be implemented by conventional devices. By way of example, output hardware may include a display terminal (e.g., a cathode ray tube (CRT)) for displaying a graphical representation of the three dimensional structure of MEK1 or a mutant or complex thereof or a portion thereof using a program such as INSIGHT (Molecular Simulations Inc., San Diego, Calif.) or QUANTA as described herein. In an embodiment of the invention, output hardware also includes a printer, so that hard copy output may be produced, or a disk drive, to store system output for later use. In an embodiment of the invention, the computer possesses a display which is displaying a three dimensional representation of MEK1 or a mutant or complex thereof or a fragment or homologue thereof.
In operation, the central processing unit (CPU) coordinates the use of the various input and output devices, coordinates data accesses from mass storage and accesses to and from working memory, and determines the sequence of data processing steps. A number of programs may be used to process the machine-readable data of this invention. Specific references to components of the computer system are included as appropriate throughout the following description of the data storage medium. A magnetic data storage medium can be encoded with a machine-readable data by a computer system as described above. Storage medium may be, for example, a conventional floppy diskette or hard disk, having a suitable substrate, which may be conventional, and a suitable coating, which may be conventional, on one or both sides, containing magnetic domains whose polarity or orientation can be altered magnetically. The magnetic domains of the coating of medium may be polarized or oriented so as to encode, in a manner which may be conventional, machine readable data, such as that described herein, for execution by a system as described herein. Storage medium may also have an opening for receiving the spindle of a disk drive or other data storage device. Alternatively, an optically-readable data storage medium can be encoded with such machine-readable data, or a set of instructions. Medium can be a conventional compact disk read only memory (CD-ROM) or a rewritable medium such as a magneto-optical disk which is optically readable and magneto-optically writable.
In general, in the case of CD-ROM, as is well known, disk coating is reflective and is impressed with a plurality of pits to encode the machine-readable data. The arrangement of the pits is read by reflecting laser light off the surface of the coating. A protective coating, which, in an embodiment of the invention, is substantially transparent, is provided on top of the coating.
In general, in the case of a magneto-optical disk, as is well known, disk coating has no pits, but has a plurality of magnetic domains whose polarity or orientation can be changed magnetically when heated above a certain temperature, as by a laser. The orientation of the domains can be read by measuring the polarization of laser light reflected from the coating. The arrangement of the domains encodes the data as described above.
Drug Design
The present invention permits the use of structure-based drug design techniques to design, select, and synthesize chemical entities, including inhibitory compounds that are capable of binding to a MEK1 or a mutant or complex thereof. De novo and iterative drug design methods can be used to develop drugs from the structure of the MEK1 crystals of this invention.
One useful drug design technique enabled by this invention is structure-based drug design. Structure-based drug design is a method for optimizing binding interactions between a protein and a compound by determining and evaluating the three-dimensional structures of successive sets of protein/compound complexes.
Those skilled in the art will appreciate that association of natural ligands or substrates with the binding pockets or hinge regions of their corresponding enzymes is the basis of many biological mechanisms of action. The term “binding pocket”, as used herein, includes any region of a molecule or molecular complex, that, as a result of its shape, favorably associates with another chemical entity or compound. In an embodiment of the invention, the binding pocket of MEK1 comprises amino acids 70-84; 93-98; 117-120; 128-129; 140-152; 193-197 and 205-208 as defined by the structural coordinates of any of Tables 2-4. The term “hinge region”, as used herein, includes the polypeptide strand that connects the two domains of the MEK1 kinase. In an embodiment of the invention, the hinge region comprises amino acids E144, H145 and M146 according to Table 1 or amino acids E143, H144 and M145 according to Table 2, 3 or 4. One of more of said binding pocket or hinge region residues can be conservatively substituted. For example, polar/hydrophilic amino acids which may be interchangeable/conservative include asparagine, glutamine, serine, cysteine, threonine, lysine, arginine, histidine, aspartic acid and glutamic acid; nonpolar/hydrophobic amino acids which may be interchangeable/conservative include glycine, alanine, valine, leucine, isoleucine, proline, tyrosine, phenylalanine, tryptophan and methionine; acidic amino acids which may be interchangeable/conservative include aspartic acid and glutamic acid and basic amino acids which may be interchangeable/conservative include histidine, lysine and arginine. Similarly, drugs may exert their biological effects through association with the binding pockets or hinge regions of enzymes. Such association may occur with all or any part of the binding pockets or hinge regions. An understanding of such associations will help lead to the design of drugs having more favorable associations with the target enzyme, and thus, improved biological effects. Therefore, this information is valuable in designing potential enzyme inhibitors, such as inhibitors of MEK1.
In iterative structure-based drug design, crystals of a series of protein/compound complexes are obtained and then the three-dimensional structure of each complex is solved. Such an approach provides insight into the association between the proteins and compounds of each complex. This is accomplished by selecting compounds with inhibitory activity, obtaining crystals of the protein complexed with each inhibitor, solving the three-dimensional structure of each complex, and comparing the protein/inhibitor interactions in each complex. By observing how changes in the compound affected the protein/compound interactions, the binding potency may be optimized. In some cases, iterative structure-based drug design is carried out by forming successive protein-compound complexes and then crystallizing each new complex. Alternatively, a pre-formed protein crystal is soaked in the presence of an inhibitor, thereby forming a protein/compound complex and obviating the need to crystallize each individual protein/compound complex. Advantageously, MEK1 crystals provided by this invention may be soaked in the presence of a compound or compounds, such as MEK1 inhibitors, substrates or other ligands to provide novel MEK1/compound crystal complexes. As used herein, the term “soaked” includes a process in which the crystal is transferred to a solution containing the compound of interest Accordingly, the present invention includes a method for making a crystal comprising amino acids 35-373 of human MEK1 polypeptide (e.g., 24-373 of SEQ ID NO: 2) complexed with a compound represented by structural formula 2:




by soaking a crystal comprising the MEK1 polypeptide complexed with ATPγS, with compound 2. In a more specific embodiment of the invention, the crystal is soaked by a process wherein about 0.1p. 1 of a 100 mM solution of said compound is combined with a drop of a solution comprising said crystal comprising said polypeptide complexed with ATPγS.

The present invention includes a soaking-based process by which any MEK1 crystal of the invention can be used to generate a crystalline composition between a MEK1 polypeptide of the invention and another ATP competitive inhibitor. Accordingly, the present invention includes a method for making a crystalline complex between an ATP competitive inhibitor and a polypeptide comprising amino acids 35-373 of MEK1 (e.g., MEK1/N35/NKF/Cdel383) comprising soaking a crystalline MEK1 composition (e.g., MEK1/N35/NKF/Cdel383-cpd2 or MEK1/N351NKF/Cdel383-ATPγS) with the ATP competitive inhibitor.
A method for identifying a MEK1 inhibitor or for evaluating the potential of a candidate MEK1 inhibitor to associate with MEK1 is within the scope of the present invention. The method comprises soaking a crystalline composition such as MEK1/N35/NKF/Cdel383-cpd2 or MEK1/N35/NKF/Cdel383-ATPγS with the candidate MEK1 inhibitor to form a complex between said polypeptide and said candidate and determining the three-dimensional structure of said complex. The candidate is considered a MEK1 inhibitor if it is shown to bind to the binding pocket or hinge region of MEK1. A candidate inhibitor that is shown to bind to MEK1 can then be confirmed to inhibit MEK1 kinase activity by subjecting it to any of the many kinase assays known in the art, e.g., as set forth below in the Examples section (see also the scintillation proximity assays (SPA) of McDonald et al., Anal. Biochem. 268:318 (1999), the in vitro assay of MacDonald et al. Molec. Cell, Biol. 13(11): 6615-6620 (1993) or coupled assays similar to those described by Jin et al., Biochemistry 35:1423-1431 (1996)).
The structure coordinates set forth in Tables 1-4 can also be used for determining at least a portion of the three-dimensional structure of molecules or molecular complexes which contain at least some structurally similar features to a MEK1 crystal of the invention. In particular, structural information about another crystallized molecule or molecular complex may be obtained by well-known techniques, including molecular replacement.
By using molecular replacement, all or part of the structure coordinates of the MEK1 polypeptide provided by this invention (and set forth in any of Tables 1-4) can be used to determine the previously unknown structure of a crystallized molecule or molecular complex more quickly and efficiently than attempting to determine such information ab initio.
Molecular replacement provides an accurate estimation of the phases for an unknown structure. Phases are a factor in equations used to solve crystal structures that cannot be measured experimentally. Obtaining accurate values for the phases, by methods other than molecular replacement, is a time-consuming process. However, when the crystal structure of a protein containing a homologous portion has been solved, the phases from the known structure may provide a satisfactory estimate of the phases for the unknown structure.
Phase information from the structure coordinates of the present invention may be used to elucidate the structure of other crystals. For example, the structure of MEK1 in complex with other atoms or molecules may be elucidated. Such complexes include, for example, those containing atoms soaked into or co-crystallized within the crystal lattice. Other structures which can be elucidated using the phase information of the present invention include for example other kinases or homologues or mutants thereof having sufficient three-dimensional structure similarity to a MEK1 complex of the invention as to be solved using molecular replacement. Also, these protein molecules in a complex with a small molecule substrate(s), inhibitor(s), transition state analog(s), product(s) or analog(s) of any of these may also be solved using the phase information of the present invention. Other complexes whose structure can be elucidated from the phase information of the present invention include a MEK1 complexed with an inhibitor. Complexes containing a combination of the above molecules may also be solved using the phase information of the present invention.
The difference Fourier method simply calculates an electron density map using phases calculated from the structure coordinates and observed diffraction amplitudes from a crystal of an unknown structure. This method is often used to solve structures of protein/ligand complexes where the ligand is small and does not affect the crystal form significantly.
An aspect of this invention provides a method of utilizing molecular replacement to obtain structural information about a crystallized molecule or molecular complex, whose structure is unknown, comprising the steps of generating an X-ray diffraction pattern from said crystallized molecule or molecular complex and applying crystallographic phases derived from at least a portion of the structure coordinates set forth in any of Tables 1-4 to the X-ray diffraction pattern to generate a three-dimensional electron density map of the molecule or molecular complex whose structure is unknown.
The scope of the present invention includes a method involving generating a preliminary model of a new molecule or molecular complex whose structure coordinates are unknown, by orienting and positioning the relevant portion of a MEK1 crystal according to any of Tables 1-4 within the unit cell of the crystal of the unknown molecule or molecular complex so as best to account for observed X-ray diffraction pattern amplitudes relating to the unknown crystal to generate an election density map of the structure whose coordinates are unknown. This, in turn, can be subjected to any well-known model building and structure refinement techniques to provide a final, accurate structure of the unknown crystallized molecule or molecular complex (Lattman, “Use of the Rotation and Translation Functions”, in Meth. Enzymol., 115: 55-77 (1985); Rossman, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York (1972)).
An embodiment of the invention also includes, for example, a structure based drug design method for evaluating the potential of a candidate MEK1 inhibitor (e.g., an ATP competitive inhibitor) to associate with: a) a polypeptide or complex thereof wherein said polypeptide comprises a binding pocket defined by structure coordinates of amino acids 70-84; 93-98; 117-120; 128-129; 140-152; 193-197 and 205-208 according to any of Tables 2-4 and/or a hinge region defined by structural coordinates of amino acids E144, H145 and M146 according to Table 1 or amino acids E143, H144 and M145 according to Table 2, 3 or 4; or b) a homologue of said polypeptide of complex thereof, wherein said homologue comprises a binding pocket or hinge region comprising a three dimensional structure characterized by structural coordinates comprising a root mean square deviation of common residue backbone atoms or alpha carbon atoms of less than about 1.5 Å (e.g., about 1 Å, about 0.75 Å, about 0.5 Å, about 0.25 Å, about 0.1 Å) when superimposed on backbone atoms or alpha carbon atoms described by structural coordinates of any of Tables 1-4 comprising the steps of: (i) employing computational means to perform a fitting operation between the candidate and the binding pocket or hinge region of the molecule or molecular complex; and (ii) analyzing the results of said fitting operation to quantify the association between the candidate and the binding pocket or hinge region. In an embodiment of the invention, the MEK1/inhibitor complex identified by structure based drug design, as set forth above, is generated experimentally and crystallized (e.g., by a method set forth herein). The three-dimensional structure of the complex is then determined by any method known in the art, for example, as set forth herein. Any inhibitor observed to bind a MEK1 polypeptide of the invention can be, as discussed above, confirmed to inhibit the kinase activity of MEK1 (e.g., by a kinase assay as set forth herein). Identification of ATP competitive inhibitors that interact with the MEK1 hinge region or a homologue thereof are preferred.
Compound 2
Compound 2 can form salts which are also within the scope of this invention. Reference to compound 2 herein is understood to include reference to salts thereof, unless otherwise indicated. The term “salt(s)”, as employed herein, includes acidic salts formed with inorganic and/or organic acids, as well as basic salts formed with inorganic and/or organic bases. Pharmaceutically acceptable (i.e., non-toxic, physiologically acceptable) salts are within the scope of the invention, although other salts are also useful. Salts of compound 2 may be formed, for example, by reacting compound 2 with an amount of acid or base, such as an equivalent amount, in a medium such as one in which the salt precipitates or in an aqueous medium followed by lyophilization.
Exemplary acid addition salts include acetates, ascorbates, benzoates, benzenesulfonates, bisulfates, borates, butyrates, citrates, camphorates, camphorsulfonates, fumarates, hydrochlorides, hydrobromides, hydroiodides, lactates, maleates, methanesulfonates, naphthalenesulfonates, nitrates, oxalates, phosphates, propionates, salicylates, succinates, sulfates, tartarates, thiocyanates, toluenesulfonates (also known as tosylates) and the like. Additionally, acids which are generally considered suitable for the formation of pharmaceutically useful salts from basic pharmaceutical compounds are discussed, for example, by S. Berge et al., Journal of Pharmaceutical Sciences (1977) 66(1) 1-19; P. Gould, International J. of Pharmaceutics (1986) 33 201-217; Anderson et al., The Practice of Medicinal Chemistry (1996), Academic Press, New York; and in The Orange Book (Food & Drug Administration, Washington, D.C. on their website). These disclosures are incorporated herein by reference thereto.
Exemplary basic salts include ammonium salts, alkali metal salts such as sodium, lithium, and potassium salts, alkaline earth metal salts such as calcium and magnesium salts, salts with organic bases (for example, organic amines) such as dicyclohexylamines, t-butyl amines, and salts with amino acids such as arginine, lysine and the like. Basic nitrogen-containing groups may be quaternized with agents such as lower alkyl halides (e.g., methyl, ethyl, and butyl chlorides, bromides and iodides), dialkyl sulfates (e.g., dimethyl, diethyl, and dibutyl sulfates), long chain halides (e.g., decyl, lauryl, and stearyl chlorides, bromides and iodides), aralkyl halides (e.g., benzyl and phenethyl bromides), and others. All such acid salts and base salts are intended to be pharmaceutically acceptable salts within the scope of the invention.
Compound 2 and salts, solvates and prodrugs thereof, may exist in their tautomeric form (for example, as an amide or imino ether). All such tautomeric forms are contemplated herein as part of the present invention.
All stereoisomers (for example, geometric isomers, optical isomers and the like) of the present compounds (including those of the salts, solvates and prodrugs of the compounds as well as the salts and solvates of the prodrugs), such as those which may exist due to asymmetric carbons on various substituents, including enantiomeric forms (which may exist even in the absence of asymmetric carbons), rotameric forms, atropisomers, and diastereomeric forms, are contemplated within the scope of this invention, as are positional isomers. Individual stereoisomers of the compounds of the invention may, for example, be substantially free of other isomers, or may be admixed, for example, as racemates or with all other, or other selected, stereoisomers. The chiral centers of the present invention can have the S or R configuration as defined by the IUPAC 1974 Recommendations. The use of the terms “salt”, “solvate” “prodrug” and the like, is intended to equally apply to the salt, solvate and prodrug of enantiomers, stereoisomers, rotamers, tautomers, positional isomers, racemates or prodrugs of the inventive compounds.
The term “patient” or “subject” includes any organism, such as an animal, for example a mammal (e.g., a human).
Compound 2 has pharmacological properties; in particular, the compound is an inhibitor of MEK1 kinase. Compound 2 is useful in the therapy of proliferative diseases such as cancer, autoimmune diseases, viral diseases, fungal diseases, neurological/neurodegenerative disorders, arthritis, inflammation, anti-proliferative (e.g., ocular retinopathy), neuronal, alopecia and cardiovascular disease. Many of these diseases and disorders are listed in U.S. Pat. No. 6,413,974, the disclosure of which is incorporated by reference herein.
More specifically, compound 2 can be useful in the treatment of a variety of cancers, including (but not limited to) the following: carcinoma, including that of the bladder, breast, colon, kidney, liver, lung, including small cell lung cancer, esophagus, gall bladder, ovary, pancreas, stomach, cervix, thyroid, prostate, and skin, including squamous cell carcinoma; hematopoietic tumors of lymphoid lineage, including leukemia, acute lymphocytic leukemia, acute lymphoblastic leukemia, B-cell lymphoma, T-cell lymphoma, Hodgkins lymphoma, non-Hodgkins lymphoma, hairy cell lymphoma and Burkeft's lymphoma; hematopoietic tumors of myeloid lineage, including acute and chronic myelogenous leukemias, myelodysplastic syndrome and promyelocytic leukemia; tumors of mesenchymal origin, including fibrosarcoma and rhabdomyosarcoma; tumors of the central and peripheral nervous system, including astrocytoma, neuroblastoma, glioma and schwannomas; and other tumors, including melanoma, seminoma, teratocarcinoma, osteosarcoma, xenoderoma pigmentosum, keratoctanthoma, thyroid follicular cancer and Kaposi's sarcoma.
Due to the key role of MEK1 in the regulation of cellular proliferation in general, inhibitors can act as reversible cytostatic agents which are useful in the treatment of any disease process which features abnormal cellular proliferation, e.g., benign prostate hyperplasia, familiar adenomatosis polyposis, neuro-fibromatosis, atherosclerosis, pulmonary fibrosis, arthritis, psoriasis, glomerulonephritis, restenosis following angioplasty or vascular surgery, hypertrophic scar formation, inflammatory bowel disease, transplantation rejection, endotoxic shock, and fungal infections.
Compound 2 is also useful in the treatment of Alzheimer's disease (see J. Biochem., (1995) 117, 741-749).
Compound 2 can induce or inhibit apoptosis. The apoptotic response is aberrant in a variety of human diseases. Compound 2, as modulators of apoptosis, is useful in the treatment of cancer (including but not limited to those types mentioned hereinabove), viral infections (including but not limited to herpesvirus, poxvirus, Epstein-Barr virus, Sindbis virus and adenovirus), prevention of AIDS development in HIV-infected individuals, autoimmune diseases (including but not limited to systemic lupus, erythematosus, autoimmune mediated glomerulonephritis, rheumatoid arthritis, psoriasis, inflammatory bowel disease, and autoimmune diabetes mellitus), neurodegenerative disorders (including but not limited to Alzheimer's disease, AIDS-related dementia, Parkinson's disease, amyotrophic lateral sclerosis, retinitis pigmentosa, spinal muscular atrophy and cerebellar degeneration), myelodysplastic syndromes, aplastic anemia, ischemic injury associated with myocardial infarctions, stroke and reperfusion injury, arrhythmia, atherosclerosis, toxin-induced or alcohol related liver diseases, hematological diseases (including but not limited to chronic anemia and aplastic anemia), degenerative diseases of the musculoskeletal system (including but not limited to osteoporosis and arthritis) aspirin-sensitive rhinosinusitis, cystic fibrosis, multiple sclerosis, kidney diseases and cancer pain.
Compound 2, as inhibitors of the MEK1, can modulate the level of cellular RNA and DNA synthesis. These agents would therefore be useful in the treatment of viral infections (including but not limited to HIV, human papilloma virus, herpesvirus, poxvirus, Epstein-Barr virus, Sindbis virus and adenovirus).
Compound 2 is useful in the chemoprevention of cancer. Chemoprevention is defined as inhibiting the development of invasive cancer by either blocking the initiating mutagenic event or by blocking the progression of pre-malignant cells that have already suffered an insult or inhibiting tumor relapse. Compound 2 is also useful in inhibiting tumor angiogenesis and metastasis.
Another aspect of this invention is a method of treating a mammal (e.g., human) having a disease or condition associated with the MEK1 by administering a therapeutically effective amount of at least one compound of Formula 2, or a pharmaceutically acceptable salt or solvate of said compound to the mammal.
In an embodiment of the invention, a therapeutically effective dosage of compound 2 or a pharmaceutically acceptable salt or solvate of said compound is about 0.001 to 500 mg/kg of body weight/day (e.g., 0.01 to 25 mg/kg of body weight/day).
The term “in association” indicates that the components of the combinations of the invention can be formulated into a single composition for simultaneous delivery or formulated separately into two or more compositions (e.g., a kit). Furthermore, each component of a combination of the invention can be administered to a subject at a different time than when the other component is administered; for example, each administration may be given non-simultaneously (e.g., separately or sequentially) at several intervals over a given period of time. Moreover, the separate components may be administered to a subject by the same or by a different route (e.g., orally, intravenously, subcutaneously).
Compound 2 is useful in association (e.g., administered together or sequentially) with one or more of anti-cancer treatments such as radiation therapy, and/or one or more anti-cancer agents selected from the group consisting of cytostatic agents, cytotoxic agents (such as for example, but not limited to, DNA interactive agents (such as cisplatin or doxorubicin)); taxanes (e.g., taxotere, taxol); topoisomerase II inhibitors (such as etoposide); topoisomerase I inhibitors (such as irinotecan (or CPT-11), camptostar, or topotecan); tubulin interacting agents (such as paclitaxel, docetaxel or the epothilones); hormonal agents (such as tamoxifen); thymidilate synthase inhibitors (such as 5-fluorouracil); anti-metabolites (such as methoxtrexate); alkylating agents (such as temozolomide (TEMODARTM from Schering-Plough Corporation, Kenilworth, N.J.), cyclophosphamide); Farnesyl protein transferase inhibitors (such as, SARASARTM (4-[2-[4-[(1-1R)-3,10-dibromo-8-chloro-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridin-11-yl-]-1-piperidinyl)-2-oxoethyl]-1-piperidinecarboxarnide, or SCH 66336 from Schering-Plough Corporation, Kenilworth, N.J.), tipifarnib (Zarnestra® or R115777 from Janssen Pharmaceuticals), L778,123 (a farnesyl protein transferase inhibitor from Merck & Company, Whitehouse Station, N.J.), BMS 214662 (a farnesyl protein transferase inhibitor from Bristol-Myers Squibb Pharmaceuticals, Princeton, N.J.); signal transduction inhibitors (such as, Iressa (from Astra Zeneca Pharmaceuticals, England), Tarceva (EGFR kinase inhibitors), antibodies to EGFR (e.g., C225), GLEEVECTM (C-abl kinase inhibitor from Novartis Pharmaceuticals, East Hanover, N.J.); interferons such as, for example, intron (from Schering-Plough Corporation), Peg-Intron (from Schering-Plough Corporation); hormonal therapy combinations; aromatase combinations; ara-C, adriamycin, cytoxan, and gemcitabine.
Other anti-cancer (also known as anti-neoplastic) agents include but are not limited to Uracil mustard, Chlormethine, Ifosfamide, Melphalan, Chlorambucil, Pipobroman, Triethylenemelamine, Triethylenethiophosphoramine, Busulfan, Carmustine, Lomustine, Streptozocin, Dacarbazine, Floxuridine, Cytarabine, 6-Mercaptopurine, 6-Thioguanine, Fludarabine phosphate, oxaliplatin, leucovirin, oxaliplatin (ELOXATINTM from Sanofi-Synthelabo Pharmaeuticals, France), Pentostatine, Vinblastine, Vincristine, Vindesine, Bleomycin, Dactinomycin, Daunorubicin, Doxorubicin, Epirubicin, Idarubicin, Mithramycin, Deoxycoformycin, Mitomycin-C, L-Asparaginase, Teniposide 17.alpha.-Ethinylestradiol, Diethylstilbestrol, Testosterone, Prednisone, Fluoxymesterone, Dromostanolone propionate, Testolactone, Megestrolacetate, Methylprednisolone, Methyltestosterone, Prednisolone, Triamcinolone, Chlorotrianisene, Hydroxyprogesterone, Aminoglutethimide, Estramustine, Medroxyprogesteroneacetate, Leuprolide, Flutamide, Toremifene, goserelin, Cisplatin, Carboplatin, Hydroxyurea, Amsacrine, Procarbazine, Mitotane, Mitoxantrone, Levamisole, Navelbene, Anastrazole, Letrazole, Capecitabine, Reloxafine, Droloxafine, or Hexamethylmelamine.
If formulated as a fixed dose, such combination products employ the compounds of this invention within the dosage range described herein and the other pharmaceutically active agent or treatment within its dosage range. For example, the scope of the present invention includes compound 2 in association with the CDC2 inhibitor olomucine (see J. Cell. Sci., (1995) 108, 2897). Compound 2 may also be administered sequentially with known anticancer or cytotoxic agents when a combination formulation is inappropriate. The invention is not limited in the sequence of administration; compound 2 may be administered either prior to or after administration of the known anticancer or cytotoxic agent. For example, the cytotoxic activity of the cyclin-dependent kinase inhibitor flavopiridol is affected by the sequence of administration with anticancer agents. Cancer Research, (1997) 57, 3375. Such techniques are within the skills of persons skilled in the art as well as attending physicians.
Accordingly, in an aspect, this invention includes combinations comprising an amount of compound 2, or a pharmaceutically acceptable salt or solvate thereof, and an amount of one or more anti-cancer treatments and/or anti-cancer agents listed above wherein the amounts of the compounds/treatments result in desired therapeutic effect.
This invention is also directed to pharmaceutical compositions which comprise compound 2 or a pharmaceutically acceptable salt or solvate of said compound and at least one pharmaceutically acceptable carrier.
For preparing pharmaceutical compositions from the compounds described by this invention, inert, pharmaceutically acceptable carriers can be either solid or liquid. Solid form preparations include, for example, powders, tablets, dispersible granules, capsules, cachets and suppositories. The powders and tablets may be comprised of, for example, from about 5 to about 95 percent active ingredient. Suitable solid carriers are known in the art, e.g., magnesium carbonate, magnesium stearate, talc, sugar or lactose. Tablets, powders, cachets and capsules can be used as solid dosage forms suitable for oral administration. Examples of pharmaceutically acceptable carriers and methods of manufacture for various compositions may be found in A. Gennaro (ed.), Remington's Pharmaceutical Sciences, 18th Edition, (1990), Mack Publishing Co., Easton, Pa.
Liquid form preparations include solutions, suspensions and emulsions. As an example may be mentioned water or water-propylene glycol solutions for parenteral injection or addition of sweeteners and opacifiers for oral solutions, suspensions and emulsions. Liquid form preparations may also include solutions for intranasal administration.
Aerosol preparations suitable for inhalation may include solutions and solids in powder form, which may be in association with a pharmaceutically acceptable carrier, such as an inert compressed gas, e.g., nitrogen.
Also included are solid form preparations that are intended to be converted, shortly before use, to liquid form preparations for either oral or parenteral administration. Such liquid forms include solutions, suspensions and emulsions.
Compound 2 of the invention may also be deliverable transdermally. The transdermal compositions can take the form of creams, lotions, aerosols and/or emulsions and can be included in a transdermal patch of the matrix or reservoir type as are conventional in the art for this purpose.
Compound 2 of this invention may also be delivered subcutaneously. In an embodiment of the invention, compound 2 is administered orally or intravenously.
In an embodiment of the invention, the pharmaceutical preparation is in a unit dosage form. In such form, the preparation is subdivided into suitably sized unit doses containing appropriate quantities of the active component, e.g., an effective amount to achieve the desired purpose.
The quantity of active compound in a unit dose of preparation may be varied or adjusted from about 1 mg to about 100 mg, e.g., from about 1 mg to about 50 mg, e.g., from about 1 mg to about 25 mg, according to the particular application.
The actual dosage employed may be varied depending upon the requirements of the patient and the severity of the condition being treated. Determination of the proper dosage regimen for a particular situation is within the skill of the art. For convenience, the total daily dosage may be divided and administered in portions during the day as required.
The amount and frequency of administration of the compounds of the invention and/or the pharmaceutically acceptable salts thereof will be regulated according to the judgment of the attending clinician considering such factors as age, condition and size of the patient as well as severity of the symptoms being treated.
Another aspect of this invention is a kit comprising a therapeutically effective amount of at least one compound of Formula 2, or a pharmaceutically acceptable salt or solvate of said compound and a pharmaceutically acceptable carrier, vehicle or diluent.
Yet another aspect of this invention is a kit comprising an amount of at least one compound of Formula 2, or a pharmaceutically acceptable salt or solvate of said compound and an amount of at least one anticancer therapy and/or anti-cancer agent listed above, wherein the amounts of the two or more ingredients result in desired therapeutic effect.
EXAMPLES
The following Examples are intended for exemplification of the present invention only and should not be construed to limit the scope of the invention. Any composition (e.g., crystal) or method disclosed in the Examples section forms part of the present invention.
Example 1
Domain Selection for MEK1 Constructs
Wild-type MEK1 has proven difficult to crystallize. This example describes the selection of the mutant MEK1 polypeptides of the invention that were used for the crystal studies set forth herein.
To chose a crystallizable domain of MEK1, the 3-dimensional structures of 20 distinct kinases were examined and divided into two classes: (A) CK2, CDK2, CDK6, ERK2, JNK & p38 have an insertion of −35 residues in the C-terminal domain and (B) PKA, calmodulin-dependent-kinase, CK1, LCK, HCK, SRC, ABL, PAK, titin kinase, twitchin kinase, FGFRTK, VEGFRTK, TGFβRTK and insulin-receptor-kinase lack this insertion. Using Clustal W, the sequences of each of these classes align well, corresponding to the structural alignment. In order to get correspondence of the sequence and structural alignments for the full 20 kinases, the −35 inserted residues must be deleted from the 6 kinases in class A.
MEK1 sequences from seven species and MEK2 sequences from five species were included in the sequence alignment to help illustrate conserved elements in the family. A Clustal W multi-sequence alignment was performed using the 7 MEK1, 5 MEK2 and the 20 distinct kinases of known structure.
From the multi-sequence analysis, the canonical kinase domain was deduced to be (55-369) MEK1. However, the construct MEK1 (55-369) was found to be completely insoluble (see Cha et al., J. Biol. Chem. 276:48494-48501 (2001)).
During purification, partial proteolysis was observed between the two serines in the sequence 236LS/SY, which is an auto-phosphorylation sequence. Large residues from the CK2 sequence were selected to replace the serines, SS->NK and to avoid phosphorylation the change Y->F was made. The triple mutant 237SSY->237NKF was observed to be resistant to proteolytic degradation and was the basis of subsequent work.
Limited tryptic and GluC digestion experimentally defined domain boundaries of MEK1 that were amenable to crystallization. Both enzymes trimmed MEK1 near the nuclear export sequence at position 35 but did not cut MEK1 at the C-terminus. Initial clones for wild-type MEK1 (2-393), and for N-terminal deletion mutants: (35-393)MEK1 and (55-393)MEK1 were constructed. MEK1 (35-393) includes a previously defined negative regulatory region which spans position 44-51 (Mansour et al., Science 265: 966-970 (1994)).
Though the canonical kinase domain (55-369) was observed to be highly insoluble, the N-terminal truncation mutant 55-393 (mentioned above), comprising residues C-terminal residues 370-393 was observed to be highly soluble. A final construct comprising a larger C-terminal domain—35-383 MEK1[237SSY->NKF]—was constructed and determined to be highly soluble.
Example 2
The Cloning of MEM N35 NKF Construct
Human MEK1 was cloned by PCR utilizing cDNA derived from human brain (Clonetech). Full length MEK1 was subcloned from pCR2.1 TOPO TA cloning vector (Invitrogen cat #K4500-01) utilizing BamH1 into pBluBacHis2 vector (Invitrogen Cat # V375-20) for baculovirus construction. The final construct was verified by sequence analysis. Three PCR primers, fTOPOI: 5ATCCCAACGACCGAAAACCTGTATTTTCAGGGCatgcccaagaagaagccgacgcccatcca gc3′ (SEQ ID NO: 3); fTOPPII: 5′CACCATGTCGTACTACCATCACCATC ACCATCACGATTACGATATCCCAACGACCGAAAACCTGTATTTTCAGGGC3′ (SEQ ID NO: 4) and rTOPO: 5TTAGACGCCAGCAGCATGGGTTGGTGTGCTGG3′ (SEQ ID NO: 5) were used sequentially to incorporate a TEV-cleavable, N-terminal His6 tag through 2 rounds of PCR amplification. Purified PCR product from the first round was used as the template for the second round of amplification. The final PCR product was incorporated into the pENTR/D-TOPO vector following the TOPO cloning instruction manual. Two PCR primers then were used to delete the N-terminal 35 amino acids fN35: 5′GCTCTAGCTCCTCCAGCTTCTTGCCCTGAAAATA CAGG3′ (SEQ ID NO: 6) and rN35: 5′CCTGTATTTTCAGGGCAAGAAGCTGGAGGAGCTAGAGC3′ (SEQ ID NO: 7), and two PCR primers fNKF: 5′GGAGGCCCCTTAACAAATTTGGAATGGACAGCCGACCTCCC3′ (SEQ ID NO: 8) and rNKF: 5′GGGAGGTCGGCTGTCCATTCCAAATTTGTTAAGGGGCCTCC3′ (SEQ ID NO: 9) were used to incorporate the NKF mutation via the Quick Change method. The final construct was verified by sequence analysis. The insert was then subcloned into the pDEST8 vector using the Gateway LR clonase reaction following the instruction manual.
Example 3
Production of Recombinant Baculoviruses (Sf9) MEK1 N35 NKF
Recombinant baculovirus was produced by utilizing the Bac-to-Bac baculovirus expression system manual (Gibco BRL, Rockville, Md., USA; SF900-II) and following the protocol for transposition, isolation of recombinant bacmid DNA, transfection of Sf9 cells with recombinant bacmid DNA and harvesting/storage of recombinant baculovirus. Recombinant virus was then plaque purified according to the Bac-to-Bac baculovirus expression system manual and amplified by the infection of suspension cultures using a multiplicity of infection of 0.05.
Example 4
Expression and Recovery of Baculovirus Recombinant MEK1 N35 NKF (High-Five)
Spodoptera frugiperda (Sf9) and Tridchopfusia ni (High FiveTM BTI-TN-5B1-4; Invitrogen, Carlsbad, Calif., USA) cells were grown in suspension at 27° C. in serum free media (SF900-II or Express Five; Gibco BRL, Rockville, Md., USA). Multiplicity of infection (MOI), cell type and time course of expression were all studied to obtain optimal protein expression yields of soluble MEK1 protein. A MOI of 5 with High-Five cells with an infection period of 48 hrs was optimal for protein expression yielding approximately 30 mg/L.
Example 5
Amino Acid Sequence of MEK1 N35 NKF
The sequence of this MEK1 N35 NKF construct expressed in High Five cells was as follows:








(SEQ ID NO: 1)



  1  MGYYHHHHHH DYDIPTTENL YFQGKKLEEL ELDEQQRKRL EAFLTQKQKV GELKDDDFEK   60



 


 61  ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY  120


 


121  GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD  180


 


181  VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG  240


 


241  LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLNKF GMDSRPPMAI  300


 


301  FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF IKRSDAEEVD  360


 


361  FAGWLCSTIG LNQPSTPTHA AGV 






Number of amino acids: 383

The molecular weight was deduced to be 42997.5 Daltons.

Example 6
Purification of MEK1 N35 NKF
The infected High Five cells were lysed in a microfluidizer in a lysis buffer (20 mM Tris pH 8.5, 10% glycerol, 5 mM (3-mercaptoethanol, 1× protease inhibitor cocktail III (Calbiochem). The lysate was centrifuged at 100,000×g for 1 hour at 4° C. The supernatant was applied to a Q-Sepharose Fast Flow column (Amersham Biosciences) equilibrated in 20 mM Tris pH 8.5, 10% glycerol, 5 mM p-mercaptoethanol. The column was washed with 20 mM Tris pH 8.5, 10% glycerol, 5 mM β-mercaptoethanol, and protein was eluted with an elution buffer (20 mM Tris pH 8.5, 10% glycerol, 5 mM 3-mercaptoethanol, 250 mM NaCl) over 10 column volumes. MEK1 protein eluted at around 125 mM NaCl. Appropriate fractions were pooled and applied to a Ni-NTA column (Qiagen) equilibrated in 20 mM Tris pH 8.0, 500 mM NaCl, 10% glycerol, and 5 mM β-mercaptoethanol. Protein was eluted with 20 mM Tris pH 8.0, 500 mM NaCl, 10% glycerol, 5 mM 3-mercaptoethanol, 150 mM imidazole over 20 column volumes. Appropriate fractions were pooled and TEV protease (Invitrogen) was added at 200 Units/mg of MEK1 and allowed to incubate overnight at 4° C. to eliminate the His-tag. The cleaved protein was applied to a second Ni-NTA column (Qiagen) which was equilibrated as described above. Appropriate fractions were pooled, diluted to  ̃2 mg/ml and dialyzed against 50 mM Tris pH 7.8, 300 mM NaCl, 10% glycerol, 0.5 mM MnCl2, 5 mM DTT for 4 hours at 4′C. Lambda phosphatase (Calbiochem) was added to the dialyzing protein at 1:450 molar ratio to remove the adventitious phosphorylation that occurs during expression. The de-phosphorylation reaction was allowed to continue in the dialysis tubing overnight at 4° C. LC-MS was used to confirm that MEK1 was completely de-phosphorylated under these conditions. The protein was concentrated to  ̃5 mg/ml and applied to a Superdex 75 (Amersham Biosciences) column equilibrated in 20 mM HEPES pH 7.5, 300 mM NaCl, 1% glycerol, 2 mM DTT, and 1 mM TCEP. Fractions containing MEK1 protein were pooled and concentrated to  ̃15 mg/ml.
Example 7
Preparation of MEK1 N35 NKF Ternary Complex (cpd.1 & ATPγS)
15 ul of a 50 mM ATPγS solution (2-fold molar excess) in the presence of 1.5 μl of (4-fold molar excess) 1M magnesium acetate stock solution was added to MEK1 N35 NFK solution (1 ml) from example 6. Compound 1 was titrated in 50 μM increments until a 1.5-fold molar excess was reached. The resulting MEK1 N35 NFK ternary complex was incubated on ice for 10 minutes than passed through a 1 μm spin filter.
Example 8
Crystallization of MEK1 N35 NKF Ternary Complex
Using a hanging-drop vapor diffusion method, the MEK1 N35 NFK ternary complex as described in example 7 (0.5 ul; 19.2 mg/ml) in 20 mM HEPES, pH 7.5, 300 mM sodium chloride, 2 mM DTT, 1 mM TCEP, 1% glycerol buffer was mixed with an equal volume of precipitant solution containing 90 mM TRIS, pH 8.5, 18% PEG 4000, 0.18 M calcium chloride and 3% DMSO as an additive component placed on the underside of a Teflon coated cover slip and sealed in close proximity to 100 μl of the precipitant solution. Crystallization plates were incubated at 4° C.; egg-shaped crystals (50×50×150 microns) grew to full size in 5-7 days. Three additional additives: 3% 1, 8-Diamino-octane, 3% Trimethylamine N-oxide, and 3% 2,2,2,-Trifluoroethanol were found to also enhance the quality and size of the resulting crystals.
Example 9
Photomicrograph of MEK1 N35 NKF Ternary Complex Crystals
As set forth above, the crystallization conditions were as follows: Protein concentration 19. 2 mg/ml, 90 mM TRIS, pH 8.5 18% PEG 4000, 0.18 M CaCl2, 3% DMSO, 4° C. A photomicrograph of the crystal obtained under these conditions was taken (FIG. 1).
Example 10
Crystallographic Analysis of MEK1 N35 NKF Ternary Complex
Prior to data collection, crystals were washed with the reservoir solution of the crystallization setup and transferred into the same solution with 20% glycerol added. The crystals were then flash-cooled in a nitrogen stream at 95 K or in liquid nitrogen, X-ray diffraction was collected using a Rigaku generator equipped with a Raxis 4 detector. Data were integrated and scaled using the HKL package.










Data collection statistics:
















Resolution
23 − 3.4 Å


No. of collected reflections
323582


No. of unique reflections (F >= 0) 
5874


R-sym
24.4%


Percent of theoretical (l/s > −3)
98%


Unit Cell
a = 77.3 Å, b = 77.3 Å, c = 221.9 Å,



α = 90°, β = 90°, γ = 120°


Space Group
P 61 2 2 (Number 78)


Asymmetric unit
1 molecule









The coordinates of the MEK1 N35 NKF-cpd.1-ATPγS ternary complex are set forth below in Table 1.
Example 11
The Cloning of MEK1 N35 NKF Cdel383 Construct
The MEK1 N35 NKF construct in pENTR/D-TOPO vector was used as a template for the generation of the MEK1 N35 NKF Cdel383 construct. Two PCR primers fCdel383:







fCdel383:


(SEQ ID NO: 10)


5′ GCAGGTTGGCTCTGCTCCACCATCGGCCTTAACCAGTAAAAGGGTGGG


 


CGCGCCGACCCAGC3′


and


 


rCdel383:


(SEQ ID NO: 11)


5′GCTGGGTCGGCGCGCCCACCCTTTTACTGGTTAAGGCCGATGGTGGAGC


 


AGAGCCAACCTGC3′ 






were used to delete the C-terminal 10 amino acids, via the Quick Change method.

Example 12
Production of Recombinant Baculoviruses (Sf9) MEK1 N35 NKF Cdel 383
Recombinant baculovirus was produced by utilizing the Bac-to-Bac baculovirus expression system manual (Gibco BRL, Rockville, Md., USA; SF900-II) and following the protocol for transposition, isolation of recombinant bacmid DNA, transfection of Sf9 cells with recombinant bacmid DNA and harvesting/storage of recombinant baculovirus. Recombinant virus was then plaque purified according to the Bac-to-Bac baculovirus expression system manual and amplified by the infection of suspension cultures using a multiplicity of infection of 0.05.
Example 13
Expression and Recovery of baculovirus Recombinant MEK1 N35 NKF Cdel 383 (Hi-Five)
Spodoptera frugiperda (Sf9) and Tridchoplusia ni(High FiveTM BTI-TN-581-4; Invitrogen, Carlsbad, Calif.) cells were grown in suspension at 27° C. in serum free media (SF900-II or Express Five; Gibco BRL, Rockville, Md., USA). Multiplicity of infection (MOD, cell type and time course of expression were all studied to obtain optimal protein expression yields of soluble MEK1 protein. A MOI of 5 with High-Five cells with an infection period of 48 hrs was optimal for protein expression yielding approximately 30 mg/L.
Example 14
Amino Acid Sequence of MEK1 N35 NKF Cdel 383








(SEQ ID NO: 2)



  1  MGYYHHHHHH DYDIPTTENL YFQGKKLEEL ELDEQQRKRL EAFLTQKQKV GELKDDDFEK   60



 


 61  ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY  120


 


121  GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD  180


 


181  VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG  240


 


241  LSLVEMAVGR YPIPPPDAKE LELMFGCQVE GDAAETPPRP RTPGRPLSSY GMDSRPPMAI  300


 


301  FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF IKRSDAEEVD  360


 


361  FAGWLCSTIG LNQ 






Number of amino acids: 373

The molecular weight was deduced to be 42079.4 Daltons.

Example 15
Purification of MEK1 N35 NKF Cdel 383
The infected High Five cells were lysed in a microfluidizer in a lysis buffer (20 mM Tris pH 8.5, 10% glycerol, 5 mM β-mercaptoethanol, 1× protease inhibitor cocktail III (Calbiochem; San Diego, Calif.). The lysate was centrifuged at 100,000×g for 1 hour at 4° C. The supernatant was applied to a Q-Sepharose Fast Flow column (Amersham Biosciences) equilibrated in 20 mM Tris pH 8.5, 10% glycerol, 5 mM β-mercaptoethanol. The column was washed with 20 mM Tris pH 8.5, 10% glycerol, 5 mM 3-mercaptoethanol, and protein was eluted with an elution buffer (20 mM Tris pH 8.5, 10% glycerol, 5 mM β-mercaptoethanol, 250 mM NaCl) over 10 column volumes. MEK1 protein eluted at around 125 mM NaCl. Appropriate fractions were pooled and applied to a Ni-NTA column (Qiagen) equilibrated in 20 mM Tris pH 8.0, 500 mM NaCl, 10% glycerol, and 5 mM β-mercaptoethanol. Protein was eluted with 20 mM Tris pH 8.0, 500 mM NaCl, 10% glycerol, 5 mM β-mercaptoethanol, 150 mM imidazole over 20 column volumes. Appropriate fractions were pooled and TEV protease (Invitrogen) was added at 200 Units/mg of MEK1 and allowed to incubate overnight at 4° C. to eliminate the His-tag. The cleaved protein was applied to a second Ni-NTA column (Qiagen) which was equilibrated as described above. Appropriate fractions were pooled, diluted to  ̃2 mg/ml and dialyzed against 50 mM Tris pH 7.8, 300 mM NaCl, 10% glycerol, 0.5 mM MnCl2, 5 mM DTT for 4 hours at 4° C. Lambda phosphatase (Calbiochem) was added to the dialyzing protein at 1:450 molar ratio to remove the adventitious phosphorylation that occurs during expression. The de-phosphorylation reaction was allowed to continue in the dialysis tubing overnight at 4° C. LC-MS was used to confirm that MEK1 was completely de-phosphorylated under these conditions. The protein was concentrated to  ̃5 mg/ml and applied to a Superdex 75 (Amersham Biosciences) column equilibrated in 20 mM HEPES pH 7.5, 300 mM NaCl, 1% glycerol, 2 mM DTT, and 1 mM TCEP. Fractions containing MEK1 protein were pooled and concentrated to  ̃10 mg/ml.
Example 16
Preparation of MEK1 N35 NKF Cdel 383 Ternary Complex (Cpd. 1 & ATPγS)
15 μl of a 50 mM ATPγS solution (2-fold molar excess) in the presence of 1.5 μl of (4-fold molar excess) 1M magnesium acetate stock solution was added to the MEK1 N35 NKF Cdel 383 solution (1 ml) as described in example 7. Compound 1 was titrated in 50 μM increments until a 1.5-fold molar excess was reached. The resulting MEK1 N35 NKF Cdel 383 ternary complex was incubated on ice for 10 minutes and filtered using a 1 μm spin filter.
Example 17
Crystallization of MEK1 N35 NKF Cdel 383 Ternary Complex
Using a hanging-drop vapor diffusion method, the MEK1 N35 NKF Cdel 383 ternary complex as described in example 16 (1 μl; 0.28 mM) in 20 mM HEPES, pH 7.5, 300 mM sodium chloride, 2 mM DTT, 1 mM TCEP, 1% glycerol buffer was mixed with an equal volume of precipitant solution containing 90 mM TRIS pH 8.5, 18% PEG 4000, 0.18 M calcium chloride and 3% DMSO placed on the underside of a siliconized Teflon slip cover and sealed in dose proximity to 100 μL of the precipitant solution. Crystallization plates were incubated at 4° C.; hexagonal rod crystals (75×75×250 microns) grew within 18-24 hours.
Example 18
Photomicrograph of MEK1 N35 NKF Cdel 383 Ternary Complex Crystals
As stated above, the crystallization conditions were as follows: protein concentration 0.28 mM, 90 mM TRIS, pH 8.5, 18% PEG 4000, 0.18 M CaCl2. 3% DMSO, 4° C. A photomicrograph of the crystals obtained was taken (FIG. 2).
Example 19
Crystallographic Analysis of MEK1 N35 NKF Cdel 383 Ternary Complex
Prior to data collection, crystals were washed with the reservoir solution of the crystallization setup and transferred into the same solution with 20% glycerol added. The crystals were then flash-cooled in a nitrogen stream at 95 K or in liquid nitrogen. X-ray diffraction was collected using a Rigaku generator equipped with a Raxis 4 detector. Data were integrated and scaled using the HKL package.










Data collection statistics:
















Resolution
32.0 − 2.2 Å


No. of collected reflections
583534


No. of unique reflections (F >= 0)
20338


R-sym
8.1%


Percent of theoretical (l/s > −3).
97.9%


Unit Cell
a = 77.1 Å, b = 77.1 Å,



c = 221.7 Å, α = β = 90°, γ = 120°


Space Group
P 61 2 2 (Number 78)


Asymmetric unit
1 molecule









The coordinates of the MEK1 N35 NKF Cdel-cpd.1-ATPγS ternary complex are set forth below in Table 2.
Example 20
MEK1 N35 NKF Cdel 383 Ternary Complex Structure Determination
The crystal structure was solved using molecular replacement. Refinement was done using the program BUSTER.


















Theoretical number of reflections 
20334




Resolution Limits
32.0 − 2.2 Å




Number of unobserved reflections
393 (1.9%)




Number of reflections in test set 
1012 (5.0%)




Number of protein residues
349




Number of solvent atoms
80




R-factor
0.215




R-free
0.246




RMSD bond length
0.011 Å




RMSD bond angles
1.054°










Example 21
Preparation of MEK1 N35 NKF Cdel 383 Binary Complex
15 ul of a 50 mM ATP-γS solution (2-fold molar excess) in the presence of 1.5 ul of (4-fold molar excess) 1M magnesium acetate stock solution was added to the MEK1N35NKFCdel383 solution (1 ml) as described in example 6. The resulting MEK1N35NKFCdel383 binary complex was incubated on ice for 10 minutes and filtered using a 1 μm spin filter.
Example 22
Crystallization and Soaking of MEK1 N35 NKF Cdel 383 Binary Complex
Using a hanging-drop vapor diffusion method, The resulting MEK1 N35 NKF Cdel383 binary complex as described in example 21 (1 μl; 0.28 mM) in 20 mM HEPES, pH 7.5, 300 mM sodium chloride, 2 mM DTT, 1 mM TCEP, 1% glycerol buffer was mixed with an equal volume of precipitant solution containing 90 mM TRIS pH 8.5, 18% PEG 4000, 0.18 M calcium chloride, 3% DMSO placed on the underside of a siliconized Teflon slip cover and sealed in close proximity to 100 μL of the precipitant solution. Crystallization plates were incubated at 4° C.; hexagonal rod crystals (75×75×250 microns) grew within 18-24 hours.
To a drop of MEK1 N35 NKF Cdel 383/ATP-γS binary crystals described above was added 0.1 ul of 100 mM compound 1 in DMSO solution. The drop was subsequently incubated at 4° C. for 13 days. A MEK1 N35 NKF Cdel 383/ATP-γS/cpd.1 ternary complex crystal was thereby generated.
Example 23
Photomicrograph of MEK1 N35 NKF Cdel 383 Binary Complex Crystals
As stated above, the crystallization conditions were as follows: protein concentration 0.28 mM, 90 mM IRIS, pH 8.5, 18% PEG 4000, 0.18 M CaCl2, DMSO, 4° C. A photomicrograph of the crystals obtained was taken (FIG. 3).
Example 24
Crystallographic Analysis of MEK1 N35 NKF Cdel 383 Binary Complex
Prior to data collection, crystals were washed with the reservoir solution of the crystallization setup and transferred into the same solution with 20% glycerol added. The crystals were then flash-cooled in a nitrogen stream at 95 K or in liquid nitrogen. X-ray diffraction was collected using a Rigaku generator equipped with a Raxis 4 detector. Data were integrated and scaled using the HKL package.










Data collection statistics:


















Resolution
39.0 − 2.45 Å



No. of collected reflections
1087533



No. of unique reflections (F >= 0)
14882



R-sym
12.5%



Percent of theoretical (l/s > −3)
97.7%



Unit Cell
a = 77.2 Å, b = 77.2 Å, c = 




222.2 Å, α = β = 90° γ = 120°



Space Group
P 61 2 2 (Number 78)



Asymmetric unit
1 molecule









The coordinates of the MEK1 N35 NKF Cdel-ATPγS binary complex are set forth below in Table 3.
Example 25
MEK1 N35 NKF Cdel383 Binary Complex Structure Determination
The crystal structure was solved using molecular replacement. Refinement was done using the program BUSTER.















Theoretical number of reflections
14882



Resolution Limits
39.0 − 2.45 Å



Number of unobserved reflections
403 (2.6%)



Number of reflections in test set
741 (5.0%)



Number of protein residues
349



R-factor
0.245



R-free
0.286



RMSD bond length
0.009 Å



RMSD bond angles
1.141°









Example 26
Preparation of MEK1 N35 NKF Cdel 383 Binary-cpd.2 Complex by Soaking and Crystallographic Analysis
To a drop of MEK1 N35 NKF Cdel 383 binary crystals as described in example 21 was added 0.1 ul of 100 mM compound 2 in DMSO solution. The drop was subsequently incubated at 4° C. for 13 days. Prior to data collection, a soaked crystal was washed with the reservoir solution of the crystallization setup and transferred into the same solution with 20% glycerol added. The crystals were then flash-cooled in a nitrogen stream at 95 K or in liquid nitrogen. X-ray diffraction was collected using a Rigaku generator equipped with a Raxis 4 detector. Data were integrated and scaled using the HKL package.










Data Collection Statistics:
















Resolution
38.0 − 2.55 Å


No. of collected reflections
643654


No. of unique reflections (F >= 0)
13285


R-sym
9.2%


Percent of theoretical (l/s > −3)
98.92%


Unit Cell
a = 76.8 Å, b = 76.8 Å,



c = 222.4 Å, α = β = 90°, γ = 120°


Space Group
P 61 2 2 (Number 78)


Asymmetric unit
1 molecule









A similar soaking procedure was carried out with




in place of compound 2 to generate a soaked MEK1 N35 NKF Cdel 383 binary—





crystalline complex (lacking ATPγS). Soluble, non-crystalline complexes including these molecules are also within the scope of the present invention.

Example 27
MEK1 N35 NKF Cdel 383 Binary-cpd.2 Complex Structure Determination (Soaking)
The crystal structure was solved using molecular replacement. Refinement was done using the program BUSTER.















Theoretical number of reflections
13285



Resolution Limits
38.0 − 2.55 Å



Number of unobserved reflections
167 (1.26%)



Number of reflections in test set
658 (5.0%)



Number of protein residues
349



R-factor
0.252



R-free
0.281



RMSD bond length
0.008 Å



RMSD bond angles
0.968°









The coordinates of the MEK1 N35 NKF Cdel-cpd.2 binary complex are set forth below in Table 4.
Example 28
Preparation of Compound 2
A compound represented by structural formula 2 can be synthesized by a method as set forth in this example.




SOCl2 (18.5 mL) was added slowly under N2 to a stirred mixture of the acid (50.0 g, 218 mmol) and pyridine (44.0 mL) in anhydrous CH2Cl2 (60 mL). The mixture was stirred at 25° C. for 20 min, then Meldrum's acid (35.0 g, 243 mmol) and DMAP (66.6 g, 546 mmol) were added and the mixture was stirred under N2 for 1 hr. Then Et2O (2 L) was added, the mixture was washed with 1 M HCl (3×500 mL), brine (500 mL), and the organic layer was dried over Na2SO4, filtered, and the solvent was evaporated. The residue was dissolved in MeOH (580 mL), and the mixture was refluxed for 4 hr. The solvent was evaporated and the residue was purified by column chromatography on silica gel with 10:1 CH2Cl2/EtOAc as eluent. Pale yellow oil (26.5 g, 43%) was obtained.




A mixture of the β-ketoester from Preparative Example 10 (20.0 g, 70.1 mmol) and 3-aminopyrazole (5.40 g, 65.0 mmol) in anhydrous toluene (60 mL) was stirred and refluxed under N2 for 24 hr. The solvent was evaporated and the residue was purified by column chromatography on silica gel with 20:1 CH2Cl2/MeOH as eluent. White solid (15.0 g, 73%) was obtained. LC-MS: 319 [M+H].




A mixture of the product from Preparative Example 20 (12.50 g, 39.3 mmol), N,N-dimethylaniline (15.5 mL), and POCl3 (125 mL) was stirred at 25° C. for 4 days. Excess of POCl3 was evaporated and the residue was poured into saturated aqueous NaNCO3 (600 mL). The mixture was extracted with CH2Cl2 (3×200 mL), the combined extracts were dried over Na2SO4, filtered, and the solvent was evaporated. The residue was purified by column chromatography on silica gel with 8:1 CH2Cl2/EtOAc as eluent. Pale yellow wax (9.41 g, 71%) was obtained. LC-MS: 337 [M+].




A solution of NBS (4.03 g, 22.7 mmol) in anhydrous CH3CN (40 mL) was added under N2 to a stirred solution of the product from Preparative Example 30 (7.63 g, 22.7 mmol) in anhydrous CH3CN (60 mL) and CH2Cl2 (20 mL). The mixture was stirred for 2 hr, the solvents were evaporated, and the residue was purified by column chromatography on silica gel with 20:1 CH2Cl2/EtOAc as eluent. Pale yellow solid foam (9.20 g, 97%) was obtained. LC-MS: 417 [M+H].




A mixture of the product from Preparative Example 40, 2.0 M NH3 in 2-propanol, and concentrated aqueous NH4OH is stirred in a closed pressure vessel at 50° C. for 2 days. The solvents are evaporated and the residue purified by column chromatography on silica gel.




TEA is added under N2 to a stirred solution of the product from Preparative Example 50 in CH2Cl2. The mixture is stirred for 1 hr, the solvent was evaporated, and the residue was mixed with solid Na2CO3 and 10:1 CH2Cl2/MeOH. The mixture is stirred under N2 for 10 min, the solution was withdrawn and loaded onto a silica gel preparative TLC plate, which is then developed with 10:1 CH2Cl2/7N NH3 in MeOH.
Example 29
Kinase Assays
A candidate that is identified to bind to a MEK1 polypeptide of the present invention by a method set forth herein can be confirmed to be a MEK1 kinase inhibitor by any of several MEK1 kinase assays known in the art. An example of an assay which can be used for this purpose is set forth in this example.
In an embodiment of the invention, the kinase activity of MEK1 in the presence of an inhibitor identified by a process as set forth herein is performed using a Biotinylated, 6-Histidine tagged fusion protein of kinase-inactive ERK2 (Biotin-His6-ERK2(K52R)) as the substrate. MEK kinase activity is assayed in the presence of activated MEK1 polypeptide (25 ng) in 20 mM HEPES (N-2-hydroxyethyl-piperazine-N′-2-ethanesulfonic acid) pH 7.5, mM MgCl2, 0.2% Octyl-β-D-Glucopyranoside, 1 mM Dithiothreitol and one of several concentrations of candidate MEK1 inhibitor. The reaction is started with the addition of 2 μM ATP, with 0.1 μCi [γ-33P] ATP and 1.4 μg Biotin-H6-ERK2(K52R). The reactions are incubated at room temperature for 60 minutes, then quenched with 10 μl 50 mM EDTA/10 mM HEPES pH 7.5 solution. The stopped reactions are transferred to a Streptavidin coated FlashPlate (NEN) and incubated one hour at room temperature to allow the Biotin-His6-ERK2(K52R) to bind to the plate. The plate is then washed 3 times with Phosphate Buffered Saline and read on a Packard Top Count NXT microplate scintillation counter. (The Ki and IC50 of a candidate inhibitor can be determined using commonly methods known in the art.







TABLE 1







Structural Coordinate of MEK1/N35/NKF (corresponding to amino acids 24, 383 


of SEQ ID NO: 1) -compound 1-ATPγS Ternary Complex.


















A
B
C
D
E
F
G
H
I
J




















ATOM
1
N
GLU
A
62
12.940
67.410
47.451
1.00
28.03


ATOM
2
CA
GLU
A
62
12.043
66.230
47.367
1.00
26.21


ATOM
3
C
GLU
A
62
10.597
66.703
47.477
1.00
28.46


ATOM
4
O
GLU
A
62
10.321
67.591
48.274
1.00
37.72


ATOM
5
CB
GLU
A
62
12.418
65.207
48.451
1.00
23.90


ATOM
6
CG
GLU
A
62
11.357
64.202
48.778
1.00
20.44


ATOM
7
CD
GLU
A
62
11.724
62.786
48.290
1.00
31.76


ATOM
8
OE1
GLU
A
62
12.349
62.022
49.092
1.00
26.74


ATOM
9
OE2
GLU
A
62
11.388
62.415
47.097
1.00
32.03


ATOM
10
N
LEU
A
63
9.660
66.119
45.734
1.00
25.92


ATOM
11
CA
LEU
A
63
8.265
66.557
46.868
1.00
24.72


ATOM
12
C
LEU
A
63
7.532
65.822
47.999
1.00
30.28


ATOM
13
O
LEU
A
63
7.437
64.596
47.986
1.00
32.99


ATOM
14
CB
LEU
A
63
7.516
66.369
45.561
1.00
27.15


ATOM
15
CG
LEU
A
63
7.092
67.660
44.866
1.00
26.66


ATOM
16
CD1
LEU
A
63
8.308
68.522
44.615
1.00
20.37


ATOM
17
CD2
LEU
A
63
6.416
67.333
43.559
1.00
19.88


ATOM
18
N
LYS
A
64
7.032
66.587
48.979
1.00
34.73


ATOM
19
CA
LYS
A
64
6.314
66.061
50.163
1.00
33.2e


ATOM
20
C
LYS
A
64
4.852
66.527
50.234
1.00
31.88


ATOM
21
O
LYS
A
64
4.489
67.558
49.665
1.00
33.72


ATOM
22
CB
LYS
A
64
7.012
66.506
51.457
1.00
34.83


ATOM
23
CG
LYS
A
64
8.334
65.814
51.749
1.00
39.38


ATOM
24
CD
LYS
A
64
8.725
65.963
53.220
1.00
39.15


ATOM
25
CE
LYS
A
64
9.104
67.394
53.560
1.00
38.49


ATOM
26
NZ
LYS
A
64
8.074
68.056
54.409
1.00
28.65


ATOM
27
N
ASP
A
65
4.019
65.788
50.960
1.00
27.94


ATOM
28
CA
ASP
A
65
2.610
66.152
51.081
1.00
27.09


ATOM
29
C
ASP
A
65
2.401
67.490
51.799
1.00
30.39


ATOM
30
O
ASP
A
65
1.569
68.307
51.384
1.00
26.56


ATOM
31
CB
ASP
A
65
1.841
65.052
51.818
1.00
28.31


ATOM
32
CG
ASP
A
65
0.369
65.404
52.029
1.00
26.42


ATOM
33
OD1
ASP
A
65
−0.271
65.977
51.121
1.00
28.69


ATOM
34
OD2
ASP
A
65
−0.157
65.097
53.112
1.00
37.08


ATOM
35
N
ASP
A
66
3.168
57.716
52.866
1.00
32.95


ATOM
36
CA
ASP
A
66
3.059
68.942
53.650
1.00
36.90


ATOM
37
C
ASP
A
66
3.490
70.222
52.950
1.00
33.30


ATOM
38
O
ASP
A
66
2.918
71.285
53.190
1.00
32.78


ATOM
39
CB
ASP
A
66
3.835
68.814
54.980
1.00
41.11


ATOM
40
CG
ASP
A
66
4.796
67.639
54.992
1.00
55.14


ATOM
41
OD1
ASP
A
66
4.465
65.567
54.429
1.00
61.63


ATOM
42
OD2
ASP
A
66
5.890
67.789
55.580
1.00
60.93


ATOM
43
N
ASP
A
67
4.482
70.127
52.072
1.00
26.09


ATOM
44
CA
ASP
A
67
4.960
71.297
51.351
1.00
19.83


ATOM
45
C
ASP
A
67
4.004
71.869
50.303
1.00
20.71


ATOM
46
O
ASP
A
67
4.411
72.730
49.522
1.00
21.95


ATOM
47
CB
ASP
A
67
6.305
70.973
50.714
1.00
24.28


ATOM
48
CG
ASP
A
67
7.344
70.566
51.744
1.00
28.79


ATOM
49
OD1
ASP
A
67
8.526
70.350
51.387
1.00
23.75


ATOM
50
OD2
ASP
A
67
6.967
70.463
52.928
1.00
32.90


ATOM
51
N
PHE
A
68
2.744
71.419
50.302
1.00
18.17


ATOM
52
CA
PHE
A
68
1.734
71.881
49.331
1.00
16.87


ATOM
53
C
PHE
A
68
0.581
72.579
50.010
1.00
17.08


ATOM
54
O
PHE
A
68
0.318
72.325
51.168
1.00
17.48


ATOM
55
CB
PHE
A
68
1.120
70.698
48.549
1.00
14.94


ATOM
56
CG
PHE
A
68
2.003
70.157
47.474
1.00
9.98


ATOM
57
CD1
PHE
A
68
2.142
70.834
46.282
1.00
7.20


ATOM
58
CD2
PHE
A
68
2.771
69.020
47.699
1.00
7.78


ATOM
59
CE1
PHE
A
68
3.045
70.398
45.331
1.00
11.25


ATOM
60
CE2
PHE
A
68
3.682
68.573
46.751
1.00
7.34


ATOM
61
CZ
PHE
A
68
3.825
69.261
45.565
1.00
2.26


ATOM
62
N
GLU
A
69
−0.136
73.417
49.270
1.00
20.41


ATOM
63
CA
GLU
A
69
−1.306
74.114
49.803
1.00
25.72


ATOM
64
C
GLU
A
69
−2.348
74.210
48.688
1.00
26.45


ATOM
65
O
GLU
A
69
−2.058
74.677
47.582
1.00
24.10


ATOM
66
CB
GLU
A
69
−0.916
75.519
50.302
1.00
33.73


ATOM
67
CG
GLU
A
69
−2.082
76.485
50.521
1.00
38.77


ATOM
68
CD
GLU
A
69
−2.027
77.702
49.590
1.00
50.74


ATOM
69
OE1
GLU
A
69
−0.919
78.054
49.120
1.00
52.97


ATOM
70
OE2
CLU
A
69
−3.092
78.311
49.329
1.00
54.17


ATOM
71
N
LYS
A
70
−3.561
73.766
48.978
1.00
25.31


ATOM
72
CA
LYS
A
70
−4.622
73.790
47.981
1.00
28.72


ATOM
73
C
LYS
A
70
−4.978
75.209
47.568
1.00
28.88


ATOM
74
O
LYS
A
70
−5.259
76.043
48.417
1.00
34.75


ATOM
75
CB
LYS
A
70
−5.872
73.086
48.527
1.00
30.22


ATOM
76
CG
LYS
A
70
−6.453
71.999
47.639
1.00
31.99


ATOM
77
CD
LYS
A
70
−6.321
70.626
48.308
1.00
39.75


ATOM
78
CE
LYS
A
70
−7.674
70.068
48.767
1.00
38.07


ATOM
79
NZ
LYS
A
70
−8.793
71.047
48.584
1.00
38.98


ATOM
80
N
ILE
A
71
−4.969
75.478
46.268
1.00
28.54


ATOM
81
CA
ILE
A
71
−5.334
76.791
45.746
1.00
27.55


ATOM
82
C
ILE
A
71
−6.775
76.709
45.246
1.00
35.03


ATOM
83
O
ILE
A
71
−7.598
77.253
45.869
1.00
36.66


ATOM
84
CB
ILE
A
71
−4.437
77.206
44.567
1.00
25.58


ATOM
85
CG1
ILE
A
71
−3.056
77.621
45.073
1.00
26.32


ATOM
86
CG2
ILE
A
71
−5.077
78.344
43.807
1.00
18.03


ATOM
87
CD1
ILE
A
71
−2.044
77.843
43.957
1.00
29.25


ATOM
88
N
SER
A
72
−6.967
76.020
44.120
1.00
37.32


ATOM
89
CA
SER
A
72
−8.292
75.843
43.532
1.00
38.96


ATOM
90
C
SER
A
72
−8.472
74.469
42.873
1.00
37.81


ATOM
91
O
SER
A
72
−7.513
73.720
42.681
1.00
42.52


ATOM
92
CB
SER
A
72
−8.562
76.941
42.513
1.00
39.00


ATOM
93
OG
SER
A
72
−8.216
76.504
41.219
1.00
49.36


ATOM
94
N
GLU
A
73
−9.712
74.145
42.533
1.00
37.27


ATOM
95
CA
GLU
A
73
−10.049
72.861
41.908
1.00
38.21


ATOM
96
C
GLU
A
73
−9.990
72.935
40.375
1.00
34.77


ATOM
97
O
GLU
A
73
−10.731
73.703
39.767
1.00
34.23


ATOM
98
CB
GLU
A
73
−11.451
72.443
42.359
1.00
38.55


ATOM
99
CG
GLU
A
73
−12.140
71.452
41.453
1.00
51.45


ATOM
100
CD
GLU
A
73
−12.088
70.042
42.004
1.00
59.57


ATOM
101
OE1
GLU
A
73
−13.130
69.349
41.951
1.00
62.16


ATOM
102
OE2
GLU
A
73
−11.006
69.632
42.492
1.00
62.93


ATOM
103
N
LEU
A
74
−9.124
72.127
39.757
1.00
31.51


ATOM
104
CA
LEU
A
74
−8.976
72.136
38.297
1.00
31.56


ATOM
105
C
LEU
A
74
−9.999
71.287
37.534
1.00
32.39


ATOM
106
O
LEU
A
74
−10.337
71.594
36.398
1.00
30.93


ATOM
107
CB
LEU
A
74
−7.562
71.692
37.916
1.00
28.71


ATOM
108
CG
LEU
A
74
−6.471
72.739
38.132
1.00
18.35


ATOM
109
CD1
LEU
A
74
−5.098
72.116
38.008
1.00
12.11


ATOM
110
CD2
LEU
A
74
−6.667
73.855
37.119
1.00
20.69


ATOM
111
N
GLY
A
75
−10.488
70.225
38.166
1.00
32.15


ATOM
112
CA
GLY
A
75
−11.461
69.360
37.537
1.00
29.95


ATOM
113
C
GLY
A
75
−11.469
68.031
38.260
1.00
37.04


ATOM
114
O
GLY
A
75
−10.642
67.802
39.155
1.00
33.34


ATOM
115
N
ALA
A
76
−12.409
67.161
37.888
1.00
41.76


ATOM
116
CA
ALA
A
76
−12.523
65.829
38.484
1.00
44.64


ATOM
117
C
ALA
A
76
−12.840
64.839
37.384
1.00
45.64


ATOM
118
O
ALA
A
76
−13.500
65.190
36.406
1.00
45.75


ATOM
119
CB
ALA
A
76
−13.625
65.800
39.527
1.00
44.36


ATOM
120
N
GLY
A
77
−12.368
63.607
37.545
1.00
45.50


ATOM
121
CA
GLY
A
77
−12.630
62.595
36.544
1.00
47.02


ATOM
122
C
GLY
A
77
−13.213
61.343
37.154
1.00
49.91


ATOM
123
O
GLY
A
77
−13.645
61.349
38.307
1.00
48.60


ATOM
124
N
ASN
A
78
−13.243
60.273
36.370
1.00
54.23


ATOM
125
CA
ASN
A
78
−13.751
58.984
36.830
1.00
58.29


ATOM
126
C
ASN
A
78
−12.739
58.499
37.856
1.00
57.46


ATOM
127
O
ASN
A
78
−12.109
57.447
37.703
1.00
54.87


ATOM
128
CB
ASN
A
78
−13.845
57.990
35.668
1.00
63.20


ATOM
129
CG
ASN
A
78
−15.273
57.749
35.223
1.00
68.90


ATOM
130
OD1
ASN
A
78
−15.811
58.481
34.385
1.00
72.57


ATOM
131
ND2
ASN
A
78
−15.899
56.714
35.780
1.00
71.42


ATOM
132
N
GLY
A
79
−12.252
59.429
38.677
1.00
56.32


ATOM
133
CA
GLY
A
79
−11.319
59.123
39.734
1.00
58.97


ATOM
134
C
GLY
A
79
−10.633
60.407
40.145
1.00
58.89


ATOM
135
O
GLY
A
79
−11.286
61.417
40.443
1.00
60.02


ATOM
136
N
GLY
A
80
−9.308
60.370
40.140
1.00
58.02


ATOM
137
CA
GLY
A
80
−8.527
61.529
40.522
1.00
54.94


ATOM
138
C
GLY
A
80
−9.133
62.902
40.305
1.00
50.91


ATOM
139
O
GLY
A
80
−9.792
63.183
39.301
1.00
48.55


ATOM
140
N
VAL
A
81
−8.943
63.755
41.301
1.00
49.95


ATOM
141
CA
VAL
A
81
−9.390
65.134
41.213
1.00
43.61


ATOM
142
C
VAL
A
81
−6.026
65.321
41.167
1.00
38.35


ATOM
143
O
VAL
A
81
−7.054
65.306
41.713
1.00
35.63


ATOM
144
CB
VAL
A
81
−10.167
65.591
42.450
1.00
42.16


ATOM
145
CG1
VAL
A
81
−9.246
65.619
43.667
1.00
41.39


ATOM
146
CG2
VAL
A
91
−10.767
66.956
42.186
1.00
33.43


ATOM
147
N
VAL
A
82
−7.964
66.957
40.499
1.00
32.69


ATOM
148
CA
VAL
A
82
−6.685
67.620
40.387
1.00
29.90


ATOM
149
C
VAL
A
82
−6.786
69.066
40.830
1.00
27.01


ATOM
150
O
VAL
A
82
−7.593
69.857
40.323
1.00
20.80


ATOM
151
CB
VAL
A
82
−6.137
67.484
38.930
1.00
33.36


ATOM
152
CG1
VAL
A
82
−7.265
67.687
37.931
1.00
37.10


ATOM
153
CG2
VAL
A
82
−4.990
68.455
38.678
1.00
20.97


ATOM
154
N
PHE
A
83
−5.953
69.393
41.804
1.00
27.74


ATOM
155
CA
PHE
A
83
−5.934
70.727
42.373
1.00
24.71


ATOM
156
C
PHE
A
83
−4.815
71.595
41.845
1.00
22.84


ATOM
157
O
PHE
A
83
−3.691
71.123
41.611
1.00
18.52


ATOM
158
CB
PHE
A
83
−5.780
70.645
43.893
1.00
25.25


ATOM
159
CG
PHE
A
83
−6.806
69.778
44.580
1.00
27.67


ATOM
160
CD1
PHE
A
83
−6.448
68.537
45.097
1.00
27.58


ATOM
161
CD2
PHE
A
83
−8.105
70.241
44.791
1.00
29.64


ATOM
162
CE1
PHE
A
83
−7.367
67.770
45.823
1.00
29.02


ATOM
163
CE2
PHE
A
83
−9.034
69.486
45.517
1.00
25.35


ATOM
164
CZ
PHE
A
83
−8.663
68.252
46.035
1.00
28.45


ATOM
165
N
LYS
A
84
−5.133
72.871
41.645
1.00
21.05


ATOM
166
CA
LYS
A
84
−4.115
73.831
41.247
1.00
22.35


ATOM
167
C
LYS
A
84
−3.497
74.103
42.614
1.00
25.67


ATOM
168
O
LYS
A
84
−4.208
74.494
43.532
1.00
25.09


ATOM
169
CB
LYS
A
84
−4.752
75.111
40.729
1.00
24.32


ATOM
170
CG
LYS
A
84
−3.888
76.329
40.947
1.00
28.32


ATOM
171
CD
LYS
A
84
−3.882
77.202
39.721
1.00
30.68


ATOM
172
CE
LYS
A
84
−4.360
78.502
40.049
1.00
27.51


ATOM
173
NZ
LYS
A
84
−3.458
79.613
39.416
1.00
33.78


ATOM
174
N
VAL
A
85
−2.200
73.881
42.778
1.00
25.76


ATOM
175
CA
VAL
A
85
−1.601
74.104
44.078
1.00
21.15


ATOM
176
C
VAL
A
85
−0.286
74.850
44.075
1.00
24.40


ATOM
177
O
VAL
A
85
0.292
75.150
43.023
1.00
23.45


ATOM
178
CB
VAL
A
85
−1.363
72.775
44.840
1.00
19.62


ATOM
179
CG1
VAL
A
85
−2.621
71.936
44.838
1.00
21.31


ATOM
180
CG2
VAL
A
85
−0.191
72.022
44.222
1.00
22.44


ATOM
181
N
SER
A
86
0.180
75.144
45.287
1.00
23.79


ATOM
182
CA
SER
A
86
1.438
75.839
45.477
1.00
19.49


ATOM
183
C
SER
A
86
2.407
74.949
46.223
1.00
10.40


ATOM
184
O
SER
A
86
2.059
74.341
47.234
1.00
13.63


ATOM
125
CB
SER
A
86
1.234
77.133
46.269
1.00
24.55


ATOM
186
OG
SER
A
86
2.115
78.148
45.811
1.00
27.54


ATOM
187
N
HIS
A
87
3.618
74.835
45.703
1.00
3.09


ATOM
188
CA
HIS
A
87
4.620
74.049
46.390
1.00
8.82


ATOM
189
C
HIS
A
87
5.360
75.108
47.245
1.00
12.24


ATOM
190
O
HIS
A
87
6.223
75.836
46.750
1.00
6.71


ATOM
191
CB
HIS
A
87
5.548
73.399
45.377
1.00
1.00


ATOM
192
CG
HIS
A
87
6.689
72.668
46.001
1.00
1.00


ATOM
193
ND2
HIS
A
87
8.006
72.938
45.688
1.00
5.69


ATOM
194
CD2
HIS
A
87
6.715
71.673
46.923
1.00
1.00


ATOM
195
CE1
HIS
A
87
8.797
72.138
46.388
1.00
5.77


ATOM
196
NE2
HIS
A
87
8.040
71.361
47.145
1.00
1.06


ATOM
197
N
LYS
A
88
5.000
75.196
48.522
1.00
13.02


ATOM
198
CA
LYS
A
88
5.573
76.202
49.423
1.00
17.36


ATOM
199
C
LYS
A
88
7.076
76.409
49.386
1.00
11.97


ATOM
200
O
LYS
A
88
7.541
77.523
49.262
1.00
13.23


ATOM
201
CB
LYS
A
88
5.124
75.934
50.858
1.00
20.83


ATOM
202
CG
LYS
A
88
3.678
76.350
51.102
1.00
28.26


ATOM
203
CD
LYS
A
88
3.221
75.984
52.508
1.00
28.97


ATOM
204
CE
LYS
A
88
3.276
74.487
52.749
1.00
29.54


ATOM
205
NZ
LYS
A
88
2.380
74.110
53.878
1.00
31.27


ATOM
206
N
PRO
A
89
7.856
75.341
49.475
1.00
9.96


ATOM
207
CA
PRO
A
89
9.299
75.568
49.441
1.00
7.23


ATOM
208
C
PRO
A
89
9.855
76.249
48.196
1.00
16.13


ATOM
209
O
PRO
A
89
10.908
76.900
48.257
1.00
23.86


ATOM
210
CB
PRO
A
89
9.893
74.175
49.630
1.00
5.49


ATOM
211
CG
PRO
A
89
8.764
73.350
50.235
1.00
1.00


ATOM
212
CD
PRO
A
89
7.514
73.921
49.638
1.00
8.19


ATOM
213
N
SER
A
90
9.357
76.146
47.082
1.00
16.18


ATOM
214
CA
SER
A
90
9.924
76.718
45.868
1.00
10.05


ATOM
215
C
SER
A
90
9.163
77.895
45.293
1.00
6.20


ATOM
215
O
SER
A
90
9.698
78.654
44.482
1.00
7.89


ATOM
217
CB
SER
A
90
10.065
75.623
44.799
1.00
10.78


ATOM
218
OG
SER
A
90
8.830
75.438
44.109
1.00
14.16


ATOM
219
N
GLY
A
91
7.914
78.047
45.701
1.00
7.82


ATOM
220
CA
GLY
A
91
7.099
79.132
45.177
1.00
10.07


ATOM
221
C
GLY
A
91
6.483
78.805
43.819
1.00
14.60


ATOM
222
O
GLY
A
91
5.726
79.600
43.255
1.00
16.52


ATOM
223
N
LEU
A
92
6.810
77.634
43.284
1.00
16.87


ATOM
224
CA
LEU
A
92
6.276
77.217
41.984
1.00
16.33


ATOM
225
C
LEU
A
92
4.819
76.830
42.076
1.00
10.17


ATOM
226
O
LEU
A
92
4.432
76.080
42.965
1.00
14.79


ATOM
227
CB
LEU
A
92
7.036
76.006
41.446
1.00
16.49


ATOM
228
CG
LEU
A
92
8.361
76.234
40.733
1.00
21.57


ATOM
229
CD1
LEU
A
92
8.965
74.884
40.321
1.00
18.61


ATOM
230
CD2
LEU
A
92
8.121
77.137
39.534
1.00
24.00


ATOM
231
N
VAL
A
93
4.005
77.355
41.174
1.00
15.27


ATOM
232
CA
VAL
A
93
2.606
76.972
41.145
1.00
19.62


ATOM
233
C
VAL
A
93
2.639
75.648
40.369
1.00
19.33


ATOM
234
O
VAL
A
93
3.328
75.546
39.367
1.00
13.93


ATOM
235
CB
VAL
A
93
1.781
77.996
40.389
1.00
24.85


ATOM
236
CG1
VAL
A
93
0.425
77.416
40.048
1.00
25.78


ATOM
237
CG2
VAL
A
93
1.625
79.234
41.239
1.00
23.46


ATOM
238
N
MET
A
94
1.942
74.627
40.847
1.00
20.57


ATOM
239
CA
MET
A
94
1.942
73.330
40.171
1.00
17.95


ATOM
240
C
MET
A
94
0.515
72.802
40.015
1.00
20.55


ATOM
241
O
MET
A
94
−0.446
73.432
40.466
1.00
22.33


ATOM
242
CB
MET
A
94
2.792
72.318
40.972
1.00
13.01


ATOM
243
CG
MET
A
94
4.288
72.662
41.016
1.00
12.46


ATOM
244
SD
MET
A
94
5.442
71.507
41.899
1.00
20.14


ATOM
245
CE
MET
A
94
4.357
70.506
42.641
1.00
14.00


ATOM
246
N
ALA
A
95
0.370
71.666
39.334
1.00
21.22


ATOM
247
CA
ALA
A
95
−0.939
71.034
39.177
1.00
15.39


ATOM
248
C
ALA
A
95
−0.709
69.739
39.913
1.00
11.16


ATOM
249
O
ALA
A
95
0.290
69.059
39.685
1.00
10.36


ATOM
250
CB
ALA
A
95
−1.260
70.779
37.722
1.00
16.97


ATOM
251
N
ARG
A
96
−1.607
69.424
40.831
1.00
10.86


ATOM
252
CA
ARG
A
96
−1.454
68.230
41.639
1.00
15.30


ATOM
253
C
ARG
A
96
−2.601
67.273
41.394
1.00
17.68


ATOM
254
O
ARG
A
96
−3.763
67.622
41.628
1.00
13.31


ATOM
255
CB
ARG
A
96
−1.409
68.593
43.123
1.00
10.74


ATOM
256
CG
ARG
A
96
−0.782
67.522
43.995
1.00
13.38


ATOM
257
CD
ARG
A
96
−1.303
67.569
45.424
1.00
9.56


ATOM
258
NE
ARG
A
96
−0.663
66.525
46.231
1.00
12.31


ATOM
259
CZ
ARG
A
96
−0.697
66.476
47.560
1.00
20.63


ATOM
260
NH1
ARG
A
96
−1.344
67.404
48.248
1.00
19.12


ATOM
261
NH2
ARG
A
96
−0.076
65.494
48.198
1.00
19.24


ATOM
262
N
LYS
A
97
−2.259
66.072
40.927
1.00
12.88


ATOM
263
CA
LYS
A
97
−3.261
65.056
40.649
1.00
12.90


ATOM
244
C
LYS
A
97
−3.255
64.014
41.750
1.00
10.35


ATOM
265
O
LYS
A
97
−2.201
63.467
42.100
1.00
5.88


ATOM
266
CB
LYS
A
97
−2.986
64.371
39.306
1.00
14.50


ATOM
267
CG
LYS
A
97
−4.206
63.451
38.755
1.00
19.32


ATOM
268
CD
LYS
A
97
−3.838
62.375
38.035
1.00
20.95


ATOM
269
CE
LYS
A
97
−3.724
62.620
36.529
1.00
21.39


ATOM
270
NZ
LYS
A
97
−5.054
62.747
35.884
1.00
17.49


ATOM
271
N
LEU
A
98
−4.439
63.755
42.300
1.00
10.40


ATOM
272
CA
LEU
A
98
−4.583
62.761
43.362
1.00
18.06


ATOM
273
C
LEU
A
98
−5.347
61.541
42.829
1.00
20.34


ATOM
274
O
LEU
A
98
−6.488
61.667
42.381
1.00
16.59


ATOM
275
CB
LEU
A
98
−5.364
63.345
44.556
1.00
18.48


ATOM
276
CG
LEU
A
98
−4.781
64.419
45.490
1.00
20.58


ATOM
277
CD1
LEU
A
98
−3.278
64.248
45.674
1.00
17.70


ATOM
278
CD2
LEU
A
98
−5.105
65.778
44.912
1.00
19.25


ATOM
279
N
ILE
A
99
−4.720
60.373
42.879
1.00
20.85


ATOM
280
CA
ILE
A
99
−5.371
59.148
42.424
1.00
22.57


ATOM
281
C
ILE
A
99
−5.527
58.292
43.658
1.00
23.36


ATOM
282
O
ILE
A
99
−4.527
57.874
44.228
1.00
23.15


ATOM
283
CB
ILE
A
99
−4.497
58.367
41.396
1.00
21.07


ATOM
284
CG1
ILE
A
99
−4.331
59.176
40.120
1.00
15.13


ATOM
285
CG2
ILE
A
99
−5.147
57.041
41.045
1.00
12.27


ATOM
286
CD1
ILE
A
99
−3.179
58.706
39.279
1.00
20.74


ATOM
287
N
HIS
A
100
−6.760
58.026
44.068
1.00
28.19


ATOM
288
CA
HIS
A
100
−6.976
57.222
45.259
1.00
38.68


ATOM
289
C
HIS
A
100
−6.171
55.939
45.207
1.00
44.03


ATOM
290
O
HIS
A
100
−4.965
55.962
45.453
1.00
51.48


ATOM
291
CB
HIS
A
100
−8.451
56.884
45.448
1.00
48.27


ATOM
292
CG
HIS
A
100
−8.786
56.403
46.831
1.00
57.92


ATOM
293
ND1
HIS
A
100
−9.109
57.263
47.862
1.00
61.52


ATOM
294
CD2
HIS
A
100
−8.860
55.153
47.351
1.00
61.56


ATOM
295
CE1
HIS
A
100
−9.366
56.560
48.953
1.00
62.93


ATOM
296
NE2
HIS
A
100
−9.222
55.279
48.670
1.00
61.73


ATOM
297
N
LEU
A
101
−6.829
54.825
44.906
1.00
44.60


ATOM
298
CA
LEU
A
101
−6.155
53.528
44.825
1.00
50.23


ATOM
299
C
LEU
A
101
−5.981
52.796
46.157
1.00
54.39


ATOM
300
O
LEU
A
101
−4.959
52.953
46.830
1.00
55.41


ATOM
301
CB
LEU
A
101
−4.772
53.678
44.172
1.00
46.54


ATOM
302
CG
LEU
A
101
−4.630
53.469
42.664
1.00
45.94


ATOM
303
CD1
LEU
A
101
−5.952
53.758
41.964
1.00
42.83


ATOM
304
CD2
LEU
A
101
−3.532
54.375
42.141
1.00
44.78


ATOM
305
N
GLU
A
102
−6.972
51.992
46.538
1.00
59.17


ATOM
306
CA
GLU
A
102
−6.881
51.214
47.770
1.00
62.37


ATOM
307
C
GLU
A
102
−5.890
50.108
47.445
1.00
63.05


ATOM
308
O
CLU
A
102
−6.278
49.016
47.022
1.00
61.68


ATOM
309
CB
GLU
A
102
−8.231
50.591
48.114
1.00
66.19


ATOM
310
CG
GLU
A
102
−9.194
51.509
48.830
1.00
69.48


ATOM
311
CD
GLU
A
102
−10.620
50.986
48.778
1.00
73.92


ATOM
312
OE1
GLU
A
102
−11.551
51.758
49.092
1.00
75.92


ATOM
313
OE2
GLU
A
102
−10.809
49.798
48.420
1.00
75.32


ATOM
314
N
ILE
A
103
−4.609
50.396
47.638
1.00
63.66


ATOM
315
CA
ILE
A
103
−3.569
49.433
47.323
1.00
63.02


ATOM
316
C
ILE
A
103
−2.514
49.276
48.421
1.00
62.06


ATOM
317
O
ILE
A
103
−2.196
50.226
49.137
1.00
60.99


ATOM
318
CB
ILE
A
103
−2.911
49.819
45.966
1.00
64.69


ATOM
319
CC1
ILE
A
103
−3.096
48.670
44.969
1.00
66.53


ATOM
320
CG2
ILE
A
103
−1.444
50.189
46.152
1.00
64.43


ATOM
321
CD1
ILE
A
103
−4.552
48.370
44.627
1.00
66.64


ATOM
322
N
LYS
A
104
−1.726
48.254
48.093
1.00
61.54


ATOM
323
CA
LYS
A
104
−0.679
47.919
49.051
1.00
60.52


ATOM
324
CB
LYS
A
104
−0.492
46.413
49.121
1.00
58.91


ATOM
325
C
LYS
A
104
0.629
48.584
48.673
1.00
61.97


ATOM
326
O
LYS
A
104
0.992
48.655
47.499
1.00
60.13


ATOM
327
N
PRO
A
105
1.359
49.078
49.675
1.00
65.06


ATOM
328
CA
PRO
A
105
2.644
49.749
49.458
1.00
57.05


ATOM
329
C
PRO
A
105
3.551
49.093
48.414
1.00
62.23


ATOM
330
O
PRO
A
105
4.335
49.774
47.754
1.00
62.64


ATOM
331
CB
PRO
A
105
3.270
49.771
50.850
1.00
66.56


ATOM
332
CG
PRO
A
105
2.077
49.836
51.774
1.00
66.22


ATOM
333
CD
PRO
A
105
0.986
49.038
51.104
1.00
65.58


ATOM
334
N
ALA
A
106
3.434
47.779
48.259
1.00
58.75


ATOM
335
CA
ALA
A
106
4.264
47.058
47.300
1.00
58.46


ATOM
336
C
ALA
A
106
4.110
47.610
45.888
1.00
58.13


ATOM
337
O
ALA
A
106
5.089
47.981
45.239
1.00
58.54


ATOM
338
CB
ALA
A
106
3.919
45.572
47.320
1.00
60.71


ATOM
339
N
ILE
A
107
2.871
47.663
45.413
1.00
55.28


ATOM
340
CA
ILE
A
107
2.598
48.157
44.078
1.00
52.31


ATOM
341
C
ILE
A
107
2.651
49.674
44.051
1.00
50.31


ATOM
342
O
ILE
A
107
3.221
50.274
43.134
1.00
46.96


ATOM
343
CB
ILE
A
107
1.215
47.657
43.569
1.00
51.94


ATOM
344
CG1
ILE
A
107
0.301
48.833
43.239
1.00
53.37


ATOM
345
CG2
ILE
A
107
0.564
46.769
44.609
1.00
48.92


ATOM
346
CD1
ILE
A
107
−0.829
48.461
42.317
1.00
54.73


ATOM
347
N
ARG
A
108
2.048
50.290
45.058
1.00
49.04


ATOM
348
CA
ARG
A
108
2.041
51.739
45.148
1.00
50.88


ATOM
349
C
ARG
A
108
3.484
52.212
44.963
1.00
50.50


ATOM
350
O
ARG
A
108
3.748
53.277
44.408
1.00
50.31


ATOM
351
CB
ARG
A
108
1.453
52.165
46.507
1.00
53.74


ATOM
352
CG
ARG
A
108
2.097
53.360
47.203
1.00
56.24


ATOM
353
CD
ARG
A
108
2.878
52.911
48.434
1.00
62.62


ATOM
354
NE
ARG
A
108
2.140
53.036
49.695
1.00
69.85


ATOM
355
CZ
ARG
A
108
1.013
52.385
49.993
1.00
72.41


ATOM
356
NH1
ARG
A
108
0.464
51.552
49.119
1.00
73.73


ATOM
357
NH2
ARG
A
108
0.441
52.546
51.181
1.00
69.61


ATOM
358
N
ASN
A
109
4.425
51.389
45.392
1.00
50.46


ATOM
359
CA
ASN
A
109
5.821
51.761
45.251
1.00
52.25


ATOM
360
C
ASN
A
109
6.312
51.470
43.840
1.00
48.73


ATOM
361
O
ASN
A
109
7.301
52.045
43.382
1.00
48.58


ATOM
362
CB
ASN
A
109
6.657
51.027
46.299
1.00
56.94


ATOM
363
CG
ASN
A
109
6.752
51.806
47.602
1.00
61.09


ATOM
364
OD1
ASN
A
109
7.593
52.696
47.743
1.00
63.41


ATOM
365
ND2
ASN
A
109
5.878
51.487
48.554
1.00
60.81


ATOM
366
N
GLN
A
110
5.606
50.580
43.154
1.00
43.67


ATOM
367
CA
GLN
A
110
5.939
50.231
41.779
1.00
38.75


ATOM
368
C
GLN
A
110
5.528
51.412
40.914
1.00
33.27


ATOM
369
O
GLN
A
110
6.290
51.902
40.074
1.00
29.57


ATOM
370
CB
GLN
A
110
5.146
49.002
41.346
1.00
42.20


ATOM
371
CG
GLN
A
110
5.994
47.798
41.036
1.00
46.47


ATOM
372
CD
GLN
A
110
6.219
47.637
39.565
1.00
49.63


ATOM
373
OE1
GLN
A
110
7.285
47.982
39.044
1.00
54.15


ATOM
374
NE2
GLN
A
110
5.214
47.110
38.872
1.00
45.60


ATOM
375
N
ILE
A
111
4.299
51.859
41.141
1.00
28.70


ATOM
376
CA
ILE
A
111
3.729
52.975
40.410
1.00
25.95


ATOM
377
C
ILE
A
111
4.623
54.193
40.542
1.00
28.35


ATOM
378
O
ILE
A
111
5.064
54.778
39.544
1.00
26.58


ATOM
379
CB
ILE
A
111
2.323
53.282
40.943
1.00
22.15


ATOM
380
CG1
ILE
A
111
1.436
52.068
40.671
1.00
19.12


ATOM
381
CG2
ILE
A
111
1.773
54.560
40.312
1.00
23.20


ATOM
382
CD1
ILE
A
111
−0.010
52.265
40.973
1.00
18.46


ATOM
383
N
ILE
A
112
4.906
54.572
41.783
1.00
30.27


ATOM
384
CA
ILE
A
112
5.769
55.719
42.025
1.00
27.04


ATOM
385
C
ILE
A
112
7.076
55.464
41.286
1.00
22.92


ATOM
386
O
ILE
A
112
7.611
56.354
40.621
1.00
19.56


ATOM
387
CB
ILE
A
112
6.061
55.900
43.543
1.00
24.82


ATOM
388
CG1
ILE
A
112
4.768
56.194
44.298
1.00
21.88


ATOM
389
CG2
ILE
A
112
7.038
57.033
43.753
1.00
23.61


ATOM
390
CD1
ILE
A
112
4.092
57.454
43.848
1.00
21.37


ATOM
391
N
ARG
A
113
7.572
54.233
41.397
1.00
24.68


ATOM
392
CA
ARG
A
113
8.827
53.844
40.761
1.00
32.12


ATOM
393
C
ARG
A
113
8.775
54.037
39.253
1.00
32.48


ATOM
394
O
ARG
A
113
9.687
54.605
38.651
1.00
31.61


ATOM
395
CB
ARG
A
113
9.142
52.380
41.087
1.00
40.11


ATOM
396
CG
ARG
A
113
10.500
51.890
40.573
1.00
47.47


ATOM
397
CD
ARG
A
113
10.621
50.359
40.667
1.00
53.84


ATOM
398
NE
ARG
A
113
9.978
49.647
39.558
1.00
60.99


ATOM
399
CZ
ARG
A
113
10.400
49.674
38.292
1.00
61.37


ATOM
400
NH1
ARG
A
113
11.475
50.383
37.967
1.00
57.24


ATOM
401
NH2
AEG
A
113
9.750
48.990
37.353
1.00
60.78


ATOM
402
N
GLU
A
114
7.698
53.563
38.641
1.00
32.96


ATOM
403
CA
GLU
A
114
7.552
53.686
37.203
1.00
32.82


ATOM
404
C
GLU
A
114
7.257
55.128
36.791
1.00
29.09


ATOM
405
O
GLU
A
114
7.623
55.552
35.694
1.00
31.16


ATOM
406
CB
GLU
A
114
6.434
52.762
36.713
1.00
35.46


ATOM
407
CG
GLU
A
114
6.780
51.276
36.748
1.00
32.07


ATOM
408
CD
GLU
A
114
5.548
50.389
36.575
1.00
33.44


ATOM
409
OE1
GLU
A
114
5.682
49.148
36.661
1.00
26.76


ATOM
410
OE2
GLU
A
114
4.445
50.938
36.356
1.00
32.15


ATOM
411
N
LEU
A
115
6.604
55.879
37.675
1.00
27.10


ATOM
412
CA
LEU
A
115
6.246
57.275
37.394
1.00
22.36


ATOM
413
C
LEU
A
115
7.469
58.173
37.263
1.00
17.92


ATOM
414
O
LEU
A
115
7.376
59.271
36.735
1.00
20.20


ATOM
415
CB
LEU
A
115
5.346
57.816
38.496
1.00
20.05


ATOM
416
CG
LEU
A
115
3.862
58.060
38.262
1.00
23.53


ATOM
417
CD1
LEU
A
115
3.373
57.359
36.998
1.00
21.23


ATOM
418
CD2
LEU
A
115
3.114
57.560
39.497
1.00
18.45


ATOM
419
N
GLN
A
116
8.613
57.696
37.737
1.00
22.74


ATOM
420
CA
GLN
A
116
9.864
58.459
37.667
1.00
24.78


ATOM
421
C
GLN
A
116
10.324
58.700
36.234
1.00
25.45


ATOM
422
O
GLN
A
116
11.097
59.628
35.963
1.00
25.15


ATOM
423
CB
GLN
A
116
10.971
57.737
38.446
1.00
28.20


ATOM
424
CG
GLN
A
116
10.715
57.643
39.945
1.00
26.03


ATOM
425
CD
GLN
A
116
10.050
58.897
40.494
1.00
28.65


ATOM
426
OE1
GLN
A
116
9.010
58.831
41.159
1.00
26.29


ATOM
427
NE2
GLN
A
116
10.648
60.048
40.208
1.00
29.16


ATOM
428
N
VAL
A
117
9.863
57.859
35.312
1.00
25.17


ATOM
429
CA
VAL
A
117
10.234
58.015
33.912
1.00
19.53


ATOM
430
C
VAL
A
117
9.818
59.396
33.420
1.00
15.32


ATOM
431
O
VAL
A
117
10.439
59.960
32.525
1.00
16.56


ATOM
432
CB
VAL
A
117
9.544
56.953
33.027
1.00
25.29


ATOM
433
CG1
VAL
A
117
9.977
57.133
31.572
1.00
14.32


ATOM
434
CG2
VAL
A
117
9.884
55.553
33.536
1.00
22.83


ATOM
435
N
LEU
A
118
6.766
59.946
34.012
1.00
15.33


ATOM
436
CA
LEU
A
118
8.283
61.251
33.604
1.00
17.15


ATOM
437
C
LEU
A
118
9.336
62.370
33.663
1.00
22.71


ATOM
438
O
LEU
A
118
9.242
63.351
32.921
1.00
26.93


ATOM
439
CB
LEU
A
118
7.031
61.600
34.416
1.00
15.11


ATOM
440
CG
LEU
A
118
5.842
60.711
34.018
1.00
14.00


ATOM
441
CD1
LEU
A
118
4.633
60.981
34.919
1.00
14.63


ATOM
442
CD2
LEU
A
118
5.482
60.931
32.558
1.00
9.57


ATOM
443
N
HIS
A
119
10.349
62.232
34.516
1.00
27.09


ATOM
444
CA
HIS
A
119
11.396
63.252
34.559
1.00
29.55


ATOM
445
C
HIS
A
119
12.154
63.291
33.259
1.00
31.74


ATOM
446
O
HIS
A
119
12.706
64.319
32.877
1.00
34.17


ATOM
447
CB
HIS
A
119
12.379
62.948
35.727
1.00
29.68


ATOM
448
CG
HIS
A
119
11.936
63.459
37.064
1.00
31.58


ATOM
449
ND1
HIS
A
119
11.756
62.632
38.156
1.00
31.57


ATOM
450
CD2
HIS
A
119
11.628
64.710
37.485
1.00
27.98


ATOM
451
CE1
HIS
A
119
11.355
63.361
39.190
1.00
30.22


ATOM
452
NE2
HIS
A
119
11.269
64.615
38.809
1.00
29.65


ATOM
453
N
GLU
A
120
12.162
62.160
32.557
1.00
35.07


ATOM
454
CA
CLU
A
120
12.845
62.026
31.269
1.00
37.51


ATOM
455
C
GLU
A
120
12.017
62.460
30.049
1.00
36.81


ATOM
456
O
GLU
A
120
12.545
62.516
28.934
1.00
35.68


ATOM
457
CB
GLU
A
120
13.298
60.574
31.066
1.00
42.16


ATOM
458
CG
GLU
A
120
14.538
60.182
31.840
1.00
49.57


ATOM
459
CD
GLU
A
120
14.733
61.019
33.090
1.00
57.79


ATOM
460
OE1
GLU
A
120
14.567
60.474
34.202
1.00
62.52


ATOM
461
OE2
GLU
A
120
15.056
62.221
32.958
1.00
62.85


ATOM
462
N
CYS
A
121
10.733
62.759
30.244
1.00
32.92


ATOM
463
CA
CYS
A
121
9.898
63.193
29.130
1.00
31.31


ATOM
464
C
CYS
A
121
9.896
64.712
29.013
1.00
33.30


ATOM
465
O
CYS
A
121
9.010
65.391
29.531
1.00
38.11


ATOM
466
CB
CYS
A
121
8.465
62.674
29.289
1.00
27.73


ATOM
467
SG
CYS
A
121
8.354
60.868
29.314
1.00
23.47


ATOM
468
N
ASN
A
122
10.507
65.239
28.335
1.00
34.97


ATOM
469
CA
ASN
A
122
11.031
66.675
28.125
1.00
35.34


ATOM
470
C
ASN
A
122
10.749
66.978
26.666
1.00
31.05


ATOM
471
O
ASN
A
122
11.443
66.482
25.776
1.00
32.36


ATOM
472
CB
ASN
A
122
12.444
67.165
28.494
1.00
38.97


ATOM
473
CG
ASN
A
122
13.107
66.307
29.558
1.00
44.55


ATOM
474
OD1
ASN
A
122
12.533
66.056
30.618
1.00
45.39


ATOM
475
ND2
ASN
A
122
14.327
65.853
29.280
1.00
49.17


ATOM
476
N
SER
A
123
9.727
67.783
26.410
1.00
26.32


ATOM
477
CA
SER
A
123
9.373
68.112
25.040
1.00
25.49


ATOM
478
C
SER
A
123
8.308
69.189
24.973
1.00
24.33


ATOM
479
O
SER
A
123
7.322
69.150
25.695
1.00
29.83


ATOM
480
CB
SER
A
123
8.866
66.864
24.305
1.00
23.27


ATOM
481
OG
SER
A
123
7.775
67.188
23.453
1.00
23.75


ATOM
482
N
PRO
A
124
8.491
70.160
24.077
1.00
23.95


ATOM
483
CA
PRO
A
124
7.546
71.263
23.898
1.00
22.67


ATOM
484
C
PRO
A
124
6.107
70.764
23.849
1.00
24.18


ATOM
485
O
PRO
A
124
5.176
71.511
24.138
1.00
27.51


ATOM
486
CB
PRO
A
124
7.943
71.871
22.560
1.00
18.59


ATOM
487
CG
PRO
A
124
9.320
71.432
22.310
1.00
17.03


ATOM
488
CD
PRO
A
124
9.645
70.255
23.171
1.00
18.47


ATOM
489
N
TYR
A
125
5.966
69.475
23.546
1.00
25.26


ATOM
490
CA
TYR
A
125
4.622
68.920
23.400
1.00
23.95


ATOM
491
C
TYR
A
125
4.116
68.061
24.552
1.00
23.69


ATOM
492
O
TYR
A
125
2.941
67.679
24.576
1.00
22.99


ATOM
493
CB
TYR
A
125
4.549
68.153
22.077
1.00
19.98


ATOM
494
CG
TYR
A
125
5.032
68.998
20.930
1.00
15.47


ATOM
495
CD1
TYR
A
125
6.297
68.516
20.383
1.00
18.77


ATOM
496
CD2
TYR
A
125
4.260
70.048
20.456
1.00
21.04


ATOM
497
CE1
TYR
A
125
6.783
69.666
19.399
1.00
19.08


ATOM
498
CE2
TYR
A
125
4.734
70.902
19.474
1.00
20.98


ATOM
499
CZ
TYR
A
125
5.991
70.707
18.955
1.00
20.25


ATOM
500
OH
TYR
A
125
6.442
71.566
17.990
1.00
30.10


ATOM
501
N
ILE
A
126
4.991
67.776
25.512
1.00
18.49


ATOM
502
CA
ILE
A
126
4.608
66.988
26.668
1.00
15.65


ATOM
503
C
ILE
A
126
4.560
67.853
27.913
1.00
15.16


ATOM
504
O
ILE
A
126
5.529
68.532
28.235
1.00
13.12


ATOM
505
CB
ILE
A
126
5.596
65.841
26.939
1.00
10.05


ATOM
506
CG1
ILE
A
126
5.548
64.819
25.804
1.00
11.19


ATOM
507
CG2
ILE
A
126
5.211
65.143
28.257
1.00
4.98


ATOM
508
CD1
ILE
A
125
4.127
64.445
25.348
1.00
10.39


ATOM
509
N
VAL
A
127
3.435
67.818
28.616
1.00
15.09


ATOM
510
CA
VAL
A
127
3.284
68.597
29.843
1.00
17.56


ATOM
511
C
VAL
A
127
4.394
68.258
30.851
1.00
16.93


ATOM
512
O
VAL
A
127
4.550
67.106
31.262
1.00
14.33


ATOM
513
CB
VAL
A
127
1.888
68.354
30.485
1.00
19.36


ATOM
514
CG1
VAL
A
127
1.818
68.996
31.873
1.00
12.30


ATOM
515
CG2
VAL
A
127
0.792
68.936
29.579
1.00
10.43


ATOM
516
N
GLY
A
128
5.166
69.279
31.232
1.00
16.61


ATOM
517
CA
GLY
A
128
6.261
69.114
32.179
1.00
13.65


ATOM
518
C
GLY
A
128
5.812
68.459
33.464
1.00
15.36


ATOM
519
O
GLY
A
128
4.717
68.719
33.951
1.00
18.98


ATOM
520
N
PHE
A
129
6.664
67.607
34.014
1.00
12.19


ATOM
521
CA
PHE
A
129
6.349
66.884
35.230
1.00
14.51


ATOM
522
C
PHE
A
129
7.355
67.281
36.289
1.00
14.64


ATOM
523
O
PHE
A
129
8.531
67.502
35.974
1.00
13.69


ATOM
524
CB
PHE
A
129
6.423
65.382
34.938
1.00
12.98


ATOM
525
CG
PHE
A
129
6.652
64.501
36.157
1.00
10.19


ATOM
526
CD1
PHE
A
129
7.923
64.021
36.452
1.00
6.81


ATOM
527
CD2
PHE
A
129
5.574
64.001
36.874
1.00
4.56


ATOM
528
CE1
PHE
A
129
8.117
63.033
37.427
1.00
7.30


ATOM
529
CE2
PHE
A
129
5.744
63.012
37.853
1.00
6.96


ATOM
530
CZ
PHE
A
129
7.016
62.522
38.128
1.00
9.00


ATOM
531
N
TYR
A
130
6.891
67.367
37.538
1.00
17.94


ATOM
532
CA
TYR
A
130
7.761
67.761
38.663
1.00
20.42


ATOM
533
C
TYR
A
130
8.056
66.615
39.634
1.00
22.08


ATOM
534
O
TYR
A
130
9.129
66.577
40.239
1.00
30.72


ATOM
535
CB
TYR
A
130
7.151
68.940
39.440
1.00
12.37


ATOM
536
CG
TYR
A
130
7.040
70.228
38.651
1.00
9.17


ATOM
537
CD1
TYR
A
130
8.174
70.859
38.134
1.00
18.25


ATOM
538
CD2
TYR
A
130
5.802
70.796
38.395
1.00
7.43


ATOM
539
CE1
TYR
A
130
8.074
72.034
37.365
1.00
15.28


ATOM
540
CE2
TYR
A
130
5.682
71.967
37.632
1.00
11.22


ATOM
541
CZ
TYR
A
130
6.818
72.576
37.114
1.00
19.64


ATOM
542
OH
TYR
A
130
6.680
73.687
36.287
1.00
23.04


ATOM
543
N
GLY
A
131
7.111
65.691
39.798
1.00
19.61


ATOM
544
CA
GLY
A
131
7.341
64.562
40.683
1.00
10.95


ATOM
545
C
GLY
A
131
6.074
63.862
41.122
1.00
15.66


ATOM
546
O
GLY
A
131
4.977
64.419
41.051
1.00
16.77


ATOM
547
N
ALA
A
132
6.232
62.629
41.593
1.00
15.34


ATOM
548
CA
ALA
A
132
5.099
61.839
42.047
1.00
16.40


ATOM
549
C
ALA
A
132
5.421
61.188
43.370
1.00
16.63


ATOM
550
O
ALA
A
132
6.547
60.740
43.600
1.00
15.99


ATOM
551
CB
ALA
A
132
4.761
60.756
41.017
1.00
18.51


ATOM
552
N
PHE
A
133
4.424
61.120
44.238
1.00
12.39


ATOM
553
CA
PHE
A
133
4.622
60.499
45.535
1.00
21.90


ATOM
554
C
PHE
A
133
3.260
60.061
46.042
1.00
26.87


ATOM
555
O
PHE
A
133
2.234
60.517
45.534
1.00
28.86


ATOM
556
CB
PHE
A
133
5.275
61.499
46.513
1.00
18.74


ATOM
557
CG
PHE
A
133
4.490
62.766
46.696
1.00
8.69


ATOM
558
CD1
PHE
A
133
3.457
62.829
47.615
1.00
10.75


ATOM
559
CD2
PHE
A
133
4.750
63.876
45.907
1.00
9.01


ATOM
560
CE1
PHE
A
133
2.678
63.991
47.747
1.00
13.73


ATOM
561
CE2
PHE
A
133
3.978
65.043
46.026
1.00
14.68


ATOM
562
CZ
PHE
A
133
2.935
65.098
46.950
1.00
10.48


ATOM
563
N
TYR
A
134
3.252
59.172
47.027
1.00
33.65


ATOM
564
CA
TYR
A
134
1.998
58.673
47.584
1.00
44.09


ATOM
565
C
TYR
A
134
1.707
59.308
42.936
1.00
46.08


ATOM
566
O
TYR
A
134
2.490
59.149
49.873
1.00
47.50


ATOM
567
CB
TYR
A
134
2.057
57.151
47.740
1.00
46.97


ATOM
568
CG
TYR
A
134
0.826
56.564
48.399
1.00
56.67


ATOM
569
CD1
TYR
A
134
0.912
55.512
49.633
1.00
57.03


ATOM
570
CD2
TYR
A
134
−0.435
56.694
47.804
1.00
59.12


ATOM
571
CE1
TYR
A
134
−0.227
55.406
50.255
1.00
60.64


ATOM
572
CE2
TYR
A
134
−1.579
56.151
48.421
1.00
60.55


ATOM
573
CZ
TYR
A
134
−1.470
55.550
49.644
1.00
61.42


ATOM
574
OH
TYR
A
134
−2.604
55.061
50.258
1.00
62.79


ATOM
575
N
SER
A
135
0.582
60.008
49.048
1.00
47.37


ATOM
576
CA
SER
A
135
0.240
60.650
50.309
1.00
48.72


ATOM
577
C
SER
A
135
−1.100
60.266
50.907
1.00
49.13


ATOM
578
O
SER
A
135
−2.159
60.567
50.353
1.00
48.45


ATOM
579
CB
SER
A
135
0.284
62.173
50.171
1.00
49.20


ATOM
580
OG
SER
A
135
−0.393
62.784
51.257
1.00
41.28


ATOM
581
N
ASP
A
136
−1.028
59.612
52.058
1.00
52.23


ATOM
582
CA
ASP
A
135
−2.194
59.192
52.821
1.00
55.18


ATOM
583
C
ASP
A
136
−3.417
58.856
51.984
1.00
52.82


ATOM
584
O
ASP
A
136
−4.360
59.646
51.897
1.00
52.40


ATOM
585
CB
ASP
A
136
−2.553
60.279
53.847
1.00
63.38


ATOM
586
CG
ASP
A
136
−1.405
60.575
54.830
1.00
71.73


ATOM
587
OD1
ASP
A
136
−1.396
59.993
55.946
1.00
74.02


ATOM
588
OD2
ASP
A
136
−0.515
61.393
54.488
1.00
72.19


ATOM
589
N
GLY
A
137
−3.475
57.601
51.551
1.00
50.78


ATOM
590
CA
GLY
A
137
−4.535
57.085
50.703
1.00
50.37


ATOM
591
C
GLY
A
137
−4.644
57.679
49.309
1.00
52.17


ATOM
592
O
GLY
A
137
−5.710
57.607
48.686
1.00
52.29


ATOM
593
N
GLU
A
138
−3.560
58.253
48.799
1.00
47.60


ATOM
594
CA
GLU
A
138
−3.620
58.841
47.476
1.00
43.63


ATOM
595
C
GLU
A
138
−2.288
59.129
46.831
1.00
40.55


ATOM
596
O
GLU
A
138
−1.550
60.004
47.276
1.00
45.45


ATOM
597
CB
GLU
A
138
−4.425
60.127
47.517
1.00
43.23


ATOM
598
CG
GLU
A
138
−5.603
60.119
46.581
1.00
48.93


ATOM
599
CD
GLU
A
138
−6.909
60.362
47.304
1.00
56.15


ATOM
600
OE1
GLU
A
138
−7.429
59.411
47.925
1.00
61.04


ATOM
601
OE2
GLU
A
138
−7.414
61.505
47.254
1.00
60.20


ATOM
602
N
ILE
A
139
−1.988
58.390
45.769
1.00
37.79


ATOM
603
CA
ILE
A
139
−0.758
58.605
45.034
1.00
32.36


ATOM
604
C
ILE
A
139
−0.881
60.009
44.450
1.00
27.26


ATOM
605
O
ILE
A
139
−1.947
60.399
43.976
1.00
30.25


ATOM
606
CB
ILE
A
139
−0.597
57.593
43.895
1.00
27.82


ATOM
607
CG1
ILE
A
139
0.638
57.948
43.072
1.00
30.64


ATOM
608
CG2
ILE
A
139
−1.839
57.587
43.022
1.00
33.34


ATOM
609
CD1
ILE
A
139
0.375
58.923
41.948
1.00
29.55


ATOM
610
N
SER
A
140
0.212
60.758
44.481
1.00
20.21


ATOM
611
CA
SER
A
140
0.212
62.132
44.000
1.00
20.04


ATOM
612
C
SER
A
140
1.156
62.352
42.835
1.00
17.48


ATOM
613
O
SER
A
140
2.266
61.819
42.838
1.00
17.20


ATOM
614
CB
SER
A
140
0.629
63.071
45.151
1.00
21.77


ATOM
615
OG
SER
A
140
−0.395
63.989
45.486
1.00
13.91


ATOM
616
N
ILE
A
141
0.719
63.152
41.855
1.00
13.87


ATOM
617
CA
ILE
A
141
1.540
63.503
40.679
1.00
16.20


ATOM
618
C
ILE
A
141
1.469
65.026
40.458
1.00
12.84


ATOM
619
O
ILE
A
141
0.378
65.608
40.387
1.00
14.10


ATOM
620
CB
ILE
A
141
1.054
62.779
39.355
1.00
14.97


ATOM
621
CG1
ILE
A
141
1.198
61.258
39.489
1.00
21.22


ATOM
622
CG2
ILE
A
141
1.891
63.230
38.167
1.00
8.79


ATOM
623
CD1
ILE
A
141
0.597
60.464
38.309
1.00
16.94


ATOM
624
N
CYS
A
142
2.627
65.665
40.328
1.00
10.20


ATOM
625
CA
CYS
A
142
2.657
67.117
40.149
1.00
10.62


ATOM
626
C
CYS
A
142
3.276
67.540
38.816
1.00
14.88


ATOM
627
O
CYS
A
142
4.394
67.119
38.423
1.00
6.78


ATOM
628
CB
CYS
A
142
3.394
67.762
41.329
1.00
12.82


ATOM
629
SG
CYS
A
142
2.998
67.001
42.948
1.00
20.75


ATOM
630
N
MET
A
143
2.544
68.395
38.119
1.00
12.04


ATOM
631
CA
MET
A
143
2.985
68.834
36.823
1.00
14.02


ATOM
632
C
MET
A
143
2.910
70.329
36.594
1.00
16.64


ATOM
633
O
MET
A
143
2.326
72.093
37.378
1.00
19.21


ATOM
634
CB
MET
A
143
2.153
68.134
35.738
1.00
17.79


ATOM
635
CG
MET
A
143
1.154
67.091
36.237
1.00
25.34


ATOM
636
SD
MET
A
143
−0.237
66.982
35.189
1.00
29.14


ATOM
637
CE
MET
A
143
−1.519
66.245
36.363
1.00
19.57


ATOM
638
N
GLU
A
144
3.512
70.731
35.486
1.00
15.71


ATOM
639
CA
GLU
A
144
3.486
72.111
35.064
1.00
17.16


ATOM
640
C
GLU
A
144
2.004
72.445
34.992
1.00
20.70


ATOM
641
O
GLU
A
144
1.192
71.626
34.548
1.00
24.10


ATOM
642
CB
GLU
A
144
4.142
72.211
33.695
1.00
15.59


ATOM
643
CG
GLU
A
144
3.577
73.246
32.755
1.00
14.63


ATOM
644
CD
GLU
A
144
4.382
73.276
31.475
1.00
18.74


ATOM
645
OE1
GLU
A
144
4.269
74.256
30.709
1.00
18.37


ATOM
646
OE2
GLU
A
144
5.143
72.306
31.244
1.00
15.77


ATOM
647
N
HIS
A
145
1.644
73.625
35.472
1.00
22.19


ATOM
648
CA
HIS
A
145
0.259
74.051
35.455
1.00
15.99


ATOM
649
C
HIS
A
145
0.067
74.617
34.057
1.00
14.93


ATOM
650
O
HIS
A
145
0.947
75.285
33.534
1.00
17.75


ATOM
651
CB
HIS
A
145
0.034
75.105
36.553
1.00
16.29


ATOM
652
CG
HIS
A
145
−1.212
75.917
36.378
1.00
19.09


ATOM
653
ND1
HIS
A
145
−2.465
75.439
36.693
1.00
23.92


ATOM
654
CD2
HIS
A
145
−1.400
77.156
35.867
1.00
18.53


ATOM
655
CE1
HIS
A
145
−3.373
76.347
36.380
1.00
17.96


ATOM
656
NE2
HIS
A
145
−2.752
77.397
35.876
1.00
12.39


ATOM
657
N
MET
A
146
−1.060
74.321
33.425
1.00
14.86


ATOM
658
CA
MET
A
146
−1.284
74.824
32.082
1.00
17.45


ATOM
659
C
MET
A
146
−2.503
75.722
32.090
1.00
21.74


ATOM
660
O
MET
A
146
−3.640
75.268
32.025
1.00
21.48


ATOM
662
CB
MET
A
146
−1.458
73.657
31.097
1.00
18.67


ATOM
652
CG
MET
A
146
−0.245
72.731
31.011
1.00
9.72


ATOM
663
SD
MET
A
146
1.165
73.392
30.043
1.00
17.17


ATOM
664
CE
MET
A
146
0.275
73.936
28.505
1.00
9.98


ATOM
665
N
ASP
A
147
−2.306
76.888
32.646
1.00
25.53


ATOM
666
CA
ASP
A
147
−3.334
77.905
32.810
1.00
30.59


ATOM
667
C
ASP
A
147
−4.414
77.982
31.743
1.00
30.67


ATOM
668
O
ASP
A
147
−5.464
78.581
31.974
1.00
31.44


ATOM
669
CB
ASP
A
147
−2.663
79.275
32.966
1.00
38.86


ATOM
670
CG
ASP
A
147
−1.876
79.687
31.741
1.00
41.29


ATOM
671
OD1
ASP
A
147
−1.534
80.883
31.640
1.00
42.35


ATOM
672
OD2
ASP
A
147
−1.600
78.822
30.882
1.00
43.11


ATOM
673
N
GLY
A
148
−4.160
77.398
30.578
1.00
32.78


ATOM
674
CA
GLY
A
148
−5.150
77.423
29.519
1.00
26.94


ATOM
675
C
GLY
A
148
−6.169
76.320
29.737
1.00
26.92


ATOM
676
O
GLY
A
148
−7.106
76.415
29.290
1.00
24.17


ATOM
677
N
GLY
A
149
−5.756
75.274
30.448
1.00
26.07


ATOM
679
CA
GLY
A
149
−6.553
74.131
30.676
1.00
26.57


ATOM
679
C
GLY
A
149
−6.544
73.045
29.655
1.00
24.46


ATOM
680
O
GLY
A
149
−5.568
72.964
28.893
1.00
23.13


ATOM
681
N
SER
A
150
−7.553
72.181
29.634
1.00
20.10


ATOM
682
CA
SER
A
150
−7.600
71.065
28.699
1.00
22.48


ATOM
683
C
SER
A
150
−8.587
71.426
27.603
1.00
25.30


ATOM
684
O
SER
A
150
−9.627
72.043
27.874
1.00
24.96


ATOM
685
CB
SER
A
150
−8.061
69.803
29.412
1.00
19.17


ATOM
686
OG
SER
A
150
−9.281
70.050
30.086
1.00
20.43


ATOM
687
N
LEU
A
151
−8.280
71.021
26.375
1.00
23.37


ATOM
686
CA
LEU
A
151
−9.127
71.354
25.235
1.00
21.64


ATOM
689
C
LEU
A
151
−10.608
71.036
25.359
1.00
20.38


ATOM
690
O
LEU
A
151
−11.412
71.656
24.681
1.00
21.59


ATOM
691
CB
LEU
A
151
−8.553
70.751
23.955
1.00
16.06


ATOM
692
CG
LEU
A
151
−7.263
71.428
23.458
1.00
17.32


ATOM
693
CD1
LEU
A
151
−6.872
70.898
22.075
1.00
17.19


ATOM
694
CD2
LEU
A
151
−7.456
72.942
23.416
1.00
16.11


ATOM
695
N
ASP
A
152
−10.993
70.090
26.206
1.00
22.86


ATOM
696
CA
ASP
A
152
−12.423
69.820
26.344
1.00
26.42


ATOM
697
C
ASP
A
152
−13.073
71.045
26.989
1.00
27.30


ATOM
698
O
ASP
A
152
−14.202
71.408
26.661
1.00
28.08


ATOM
699
CB
ASP
A
152
−12.689
68.575
27.197
1.00
28.72


ATOM
700
CG
ASP
A
152
−12.110
68.689
28.584
1.00
34.12


ATOM
701
OD1
ASP
A
152
−12.877
68.558
29.566
1.00
35.49


ATOM
702
OD2
ASP
A
152
−10.885
68.907
28.688
1.00
36.66


ATOM
703
N
GLN
A
153
−12.359
71.689
27.904
1.00
27.94


ATOM
704
CA
GLN
A
153
−12.897
72.889
28.536
1.00
31.58


ATOM
708
C
GLN
A
153
−12.938
74.004
27.475
1.00
30.22


ATOM
706
O
GLN
A
153
−13.976
74.628
27.256
1.00
29.34


ATOM
707
CB
GLN
A
153
−12.028
73.318
29.731
1.00
31.94


ATOM
708
CG
GLN
A
153
−11.277
72.185
30.436
1.00
37.31


ATOM
709
CD
GLN
A
153
−10.540
72.645
31.698
1.00
38.91


ATOM
710
OE1
GLN
A
153
−9.300
72.630
31.769
1.00
33.30


ATOM
711
NE2
GLN
A
153
−11.302
73.052
32.698
1.00
40.65


ATOM
712
N
VAL
A
154
−11.807
74.235
26.813
1.00
29.11


ATOM
713
CA
VAL
A
154
−11.711
75.258
25.773
1.00
24.82


ATOM
714
C
VAL
A
154
−12.799
05.077
24.711
1.00
30.19


ATOM
715
O
VAL
A
154
−13.282
76.045
24.133
1.00
32.86


ATOM
716
CB
VAL
A
154
−10.319
75.224
25.096
1.00
22.46


ATOM
717
CG1
VAL
A
154
−10.233
76.261
23.985
1.00
15.50


ATOM
718
CG2
VAL
A
154
−9.243
75.471
26.134
1.00
8.68


ATOM
719
N
LEU
A
155
−13.190
73.832
24.460
1.00
33.07


ATOM
720
CA
LEU
A
155
−14.223
73.537
23.474
1.00
30.20


ATOM
721
C
LEU
A
155
−15.603
73.907
24.002
1.00
30.50


ATOM
722
O
LEU
A
155
−16.462
74.347
23.243
1.00
34.91


ATOM
723
CB
LEU
A
155
−14.203
72.049
23.116
1.00
30.99


ATOM
724
CG
LEU
A
155
−14.874
71.561
21.824
1.00
29.65


ATOM
725
CD1
LEU
A
155
−16.327
71.296
22.097
1.00
31.20


ATOM
726
CD2
LEU
A
155
−14.712
72.582
20.711
1.00
26.00


ATOM
727
N
LYS
A
156
−15.824
73.716
25.300
1.00
28.46


ATOM
728
CA
LYS
A
156
−17.116
74.043
25.894
1.00
29.48


ATOM
729
CB
LYS
A
156
−17.193
73.545
27.333
1.00
20.91


ATOM
730
C
LYS
A
156
−17.308
75.551
25.848
1.00
34.24


ATOM
731
O
LYS
A
156
−18.392
76.039
25.508
1.00
39.12


ATOM
732
N
LYS
A
150
−16.249
76.290
26.171
1.00
35.95


ATOM
733
CA
LYS
A
157
−16.300
77.746
26.163
1.00
35.68


ATOM
734
CB
LYS
A
157
−15.337
78.314
27.210
1.00
29.27


ATOM
735
C
LYS
A
157
−15.974
78.316
24.785
1.00
40.65


ATOM
736
O
LYS
A
157
−15.614
79.483
24.665
1.00
44.71


ATOM
737
N
ALA
A
158
−16.100
77.497
23.744
1.00
45.65


ATOM
738
CA
ALA
A
158
−15.808
77.949
22.381
1.00
45.62


ATOM
739
C
ALA
A
158
−16.686
77.293
21.326
1.00
47.53


ATOM
740
O
ALA
A
158
−16.452
77.476
20.133
1.00
50.88


ATOM
741
CB
ALA
A
158
−14.335
77.698
22.042
1.00
47.87


ATOM
742
N
GLY
A
159
−17.686
75.527
21.762
1.00
46.73


ATOM
743
CA
GLY
A
159
−18.574
75.856
20.823
1.00
46.87


ATOM
744
C
GLY
A
159
−17.832
74.855
19.955
1.00
46.86


ATOM
745
O
GLY
A
159
−17.867
73.648
20.211
1.00
45.56


ATOM
746
N
ARG
A
160
−17.169
75.366
18.917
1.00
45.69


ATOM
747
CA
ARG
A
160
−16.375
74.545
18.009
1.00
44.28


ATOM
748
C
ARG
A
160
−15.090
75.313
17.746
1.00
39.43


ATOM
749
O
ARG
A
160
−15.122
76.519
17.529
1.00
41.84


ATOM
750
CB
ARG
A
160
−17.137
74.282
16.701
1.00
45.12


ATOM
751
CG
ARG
A
160
−17.023
75.370
18.662
1.00
45.97


ATOM
752
CD
ARG
A
160
−18.397
75.874
15.259
1.00
55.74


ATOM
753
NE
ARG
A
160
−18.937
75.165
14.103
1.00
61.36


ATOM
754
CZ
ARG
A
160
−18.907
75.629
12.854
1.00
66.31


ATOM
755
NH1
ARG
A
160
−18.361
76.814
12.588
1.00
62.96


ATOM
756
NH2
ARG
A
160
−19.423
74.904
11.866
1.00
65.23


ATOM
757
N
ILE
A
161
−13.957
74.626
17.804
1.00
35.92


ATOM
758
CA
ILE
A
161
−12.679
75.272
17.565
1.00
31.37


ATOM
759
C
ILE
A
161
−12.464
75.362
16.054
1.00
35.54


ATOM
760
O
ILE
A
161
−12.842
74.463
15.314
1.00
37.48


ATOM
761
CB
ILE
A
161
−11.550
74.494
18.268
1.00
26.70


ATOM
762
CG1
ILE
A
161
−11.609
74.790
19.774
1.00
25.16


ATOM
763
CG2
ILE
A
161
−10.202
74.905
17.741
1.00
24.00


ATOM
764
CD1
ILE
A
161
−10.870
73.795
20.652
1.00
21.33


ATOM
765
N
PRO
A
162
−11.891
76.477
15.574
1.00
37.44


ATOM
766
CA
PRO
A
162
−11.623
76.716
14.149
1.00
35.38


ATOM
767
C
PRO
A
162
−10.532
75.857
13.529
1.00
34.79


ATOM
768
O
PRO
A
162
−9.524
75.537
14.168
1.00
37.94


ATOM
769
CB
PRO
A
162
−11.263
78.199
14.079
1.00
34.53


ATOM
770
CG
PRO
A
162
−11.522
78.755
15.452
1.00
37.13


ATOM
771
CD
PRO
A
162
−11.461
77.611
16.404
1.00
39.70


ATOM
772
N
GLU
A
163
−10.833
75.524
12.140
1.00
32.34


ATOM
773
CA
GLU
A
163
−9.912
74.675
11.409
1.00
35.84


ATOM
774
C
GLU
A
163
−8.456
75.119
11.487
1.00
36.46


ATOM
775
O
GLU
A
163
−7.557
74.297
11.636
1.00
40.80


ATOM
776
CB
GLU
A
163
−10.339
74.587
9.949
1.00
35.27


ATOM
777
CG
GLU
A
163
−9.442
73.709
9.131
1.00
35.84


ATOM
778
CD
GLU
A
163
−9.864
73.639
7.689
1.00
38.55


ATOM
779
OE1
GLU
A
163
−10.958
74.149
7.357
1.00
42.91


ATOM
780
OE2
GLU
A
163
−9.094
73.072
6.888
1.00
38.53


ATOM
781
N
GLN
A
164
−8.214
76.418
11.388
1.00
36.63


ATOM
782
CA
GLN
A
164
−6.846
76.909
11.442
1.00
37.30


ATOM
783
C
GLN
A
164
−6.178
76.558
12.771
1.00
36.11


ATOM
784
O
GLN
A
164
−5.021
76.126
12.805
1.00
35.86


ATOM
785
CB
GLN
A
164
−6.828
78.420
11.212
1.00
39.53


ATOM
786
CG
GLN
A
164
−5.789
78.866
10.203
1.00
43.05


ATOM
787
CD
GLN
A
164
−6.387
79.141
8.841
1.00
49.30


ATOM
788
OE1
GLN
A
164
−7.253
80.006
8.693
1.00
47.73


ATOM
789
NE2
GLN
A
164
−5.932
78.402
7.830
1.00
48.05


ATOM
790
N
ILE
A
165
−6.911
76.736
13.863
1.00
34.47


ATOM
791
CA
ILE
A
165
−6.388
76.429
15.186
1.00
35.29


ATOM
792
C
ILE
A
165
−6.384
74.252
15.832
1.00
32.10


ATOM
793
O
ILE
A
165
−5.337
74.385
15.930
1.00
28.56


ATOM
794
CB
ILE
A
165
−7.255
77.091
16.276
1.00
37.53


ATOM
795
CG1
ILE
A
165
−6.766
78.519
16.501
1.00
35.01


ATOM
796
CG2
ILE
A
165
−7.161
76.329
17.586
1.00
40.94


ATOM
797
CD1
ILE
A
165
−7.857
79.526
16.433
1.00
38.89


ATOM
798
N
LEU
A
166
−7.326
74.194
14.914
1.00
33.23


ATOM
799
CA
LEU
A
166
−7.299
72.744
15.018
1.00
30.09


ATOM
800
C
LEU
A
166
−6.073
72.249
14.257
1.00
30.60


ATOM
801
O
LEU
A
166
−5.580
71.149
14.500
1.00
32.76


ATOM
802
CB
LEU
A
166
−8.574
72.145
14.426
1.00
28.10


ATOM
803
CG
LEU
A
166
−9.782
72.301
15.353
1.00
27.13


ATOM
804
CD1
LEU
A
166
−10.960
71.453
14.844
1.00
20.97


ATOM
805
CD2
LEU
A
166
−9.363
71.901
16.774
1.00
19.88


ATOM
806
N
GLY
A
167
−5.578
73.060
13.339
1.00
32.63


ATOM
807
CA
GLY
A
167
−4.405
72.722
12.563
1.00
30.17


ATOM
808
C
GLY
A
167
−3.154
72.753
13.422
1.00
30.43


ATOM
609
O
GLY
A
167
−2.296
71.872
13.324
1.00
30.93


ATOM
810
N
LYS
A
168
−3.046
73.772
14.268
1.00
31.57


ATOM
811
CA
LYS
A
168
−1.896
73.898
15.156
1.00
30.89


ATOM
812
CB
LYS
A
168
−1.877
75.276
15.807
1.00
27.56


ATOM
613
C
LYS
A
168
−1.952
72.798
16.221
1.00
32.22


ATOM
814
O
LYS
A
168
−0.912
72.258
16.623
1.00
35.68


ATOM
815
N
VAL
A
169
−3.165
72.456
16.664
1.00
28.88


ATOM
816
CA
VAL
A
169
−3.353
71.408
17.670
1.00
19.89


ATOM
617
C
VAL
A
169
−2.815
70.089
17.127
1.00
21.63


ATOM
818
O
VAL
A
169
−2.073
69.366
17.807
1.00
21.58


ATOM
819
CB
VAL
A
169
−4.845
71.234
18.026
1.00
18.98


ATOM
820
CG1
VAL
A
169
−5.029
70.037
18.981
1.00
14.97


ATOM
821
CG2
VAL
A
169
−5.375
72.516
18.665
1.00
14.52


ATOM
822
N
SER
A
170
−3.188
69.792
15.886
1.00
20.33


ATOM
823
CA
SER
A
170
−2.752
68.570
15.230
1.00
17.37


ATOM
824
C
SER
A
170
−1.229
68.501
15.219
1.00
17.09


ATOM
825
O
SER
A
170
−0.657
67.499
15.629
1.00
20.61


ATOM
826
CB
SER
A
170
−3.313
68.505
13.810
1.00
19.84


ATOM
827
OG
SER
A
170
−4.733
68.533
13.823
1.00
19.10


ATOM
828
N
ILE
A
171
−0.568
69.560
14.763
1.00
17.15


ATOM
829
CA
ILE
A
171
0.889
69.576
14.752
1.00
17.81


ATOM
830
C
ILE
A
171
1.422
69.204
16.148
1.00
17.91


ATOM
831
O
ILE
A
171
2.322
68.369
16.276
1.00
16.55


ATOM
832
CB
ILE
A
171
1.432
70.968
14.325
1.00
18.36


ATOM
833
CG1
ILE
A
171
1.401
71.086
12.808
1.00
24.02


ATOM
834
CG2
ILE
A
171
2.876
71.135
14.757
1.00
23.10


ATOM
835
CD1
ILE
A
171
0.739
72.329
12.304
1.00
31.26


ATOM
836
N
ALA
A
172
0.838
69.800
17.190
1.00
15.52


ATOM
837
CA
ALA
A
172
1.249
69.527
18.575
1.00
15.61


ATOM
838
C
ALA
A
172
1.034
68.080
18.994
1.00
14.16


ATOM
839
O
ALA
A
172
1.949
67.443
19.528
1.00
12.15


ATOM
840
CB
ALA
A
172
0.499
70.451
19.535
1.00
18.77


ATOM
841
N
VAL
A
173
−0.179
67.570
18.770
1.00
13.42


ATOM
842
CA
VAL
A
173
−0.505
66.187
19.128
1.00
15.18


ATOM
843
C
VAL
A
173
0.438
65.216
18.429
1.00
17.01


ATOM
844
O
VAL
A
173
0.984
64.319
19.062
1.00
23.77


ATOM
845
CB
VAL
A
173
−1.975
65.791
18.750
1.00
14.24


ATOM
846
CG1
VAL
A
173
−2.186
64.291
18.935
1.00
5.50


ATOM
847
CG2
VAL
A
173
−2.964
66.547
19.594
1.00
7.97


ATOM
848
N
ILE
A
174
0.634
65.388
17.128
1.00
19.25


ATOM
849
CA
ILE
A
174
1.521
64.488
16.400
1.00
21.80


ATOM
850
C
ILE
A
174
2.990
64.650
16.803
1.00
21.26


ATOM
851
O
ILE
A
174
3.664
63.659
17.038
1.00
21.58


ATOM
852
CB
ILE
A
174
1.373
64.641
14.865
1.00
25.48


ATOM
853
CG1
ILE
A
174
2.598
64.064
14.160
1.00
32.34


ATOM
854
CG2
ILE
A
174
1.239
66.078
14.499
1.00
31.40


ATOM
855
CD1
ILE
A
174
2.416
62.629
13.686
1.00
41.26


ATOM
856
N
LYS
A
175
3.498
65.877
16.894
1.00
19.28


ATOM
857
CA
LYS
A
175
4.895
66.044
17.308
1.00
22.09


ATOM
858
C
LYS
A
175
5.060
65.390
18.681
1.00
19.31


ATOM
859
O
LYS
A
176
6.114
64.839
19.013
1.00
17.73


ATOM
860
CB
LYS
A
175
5.262
67.523
17.391
1.00
24.23


ATOM
861
CG
LYS
A
175
5.107
68.252
16.063
1.00
27.00


ATOM
862
CD
LYS
A
175
6.432
68.455
15.364
1.00
24.86


ATOM
663
CE
LYS
A
175
6.914
69.890
15.515
1.00
35.11


ATOM
864
NZ
LYS
A
175
6.920
70.633
14.222
1.00
31.01


ATOM
865
N
GLY
A
176
3.989
65.449
19.469
1.00
18.02


ATOM
866
CA
GLY
A
176
3.992
64.854
20.795
1.00
14.51


ATOM
867
C
GLY
A
176
4.023
63.334
20.806
1.00
14.32


ATOM
868
O
GLY
A
176
4.889
62.720
21.445
1.00
12.68


ATOM
869
N
LEU
A
177
3.075
62.710
20.109
1.00
13.29


ATOM
870
CA
LEU
A
177
3.038
61.252
20.059
1.00
11.02


ATOM
871
C
LEU
A
177
4.321
60.664
19.469
1.00
12.05


ATOM
872
O
LEU
A
177
4.794
59.622
19.940
1.00
14.19


ATOM
873
CB
LEU
A
177
1.819
60.783
19.264
1.00
5.55


ATOM
874
CG
LEU
A
177
0.503
61.029
19.988
1.00
4.04


ATOM
875
CD1
LEU
A
177
−0.624
61.254
19.005
1.00
13.14


ATOM
876
CD2
LEU
A
177
0.210
59.844
20.845
1.00
13.50


ATOM
877
N
THR
A
178
4.918
61.326
18.470
1.00
18.26


ATOM
372
CA
THR
A
178
6.137
60.762
17.884
1.00
20.52


ATOM
879
C
THR
A
178
7.351
60.894
18.804
1.00
23.30


ATOM
880
O
THR
A
178
8.269
60.060
18.750
1.00
21.43


ATOM
881
CB
THR
A
178
6.439
61.323
16.442
1.00
17.29


ATOM
882
OG1
THR
A
178
7.805
61.733
16.342
1.00
22.66


ATOM
883
CG2
THR
A
178
5.561
62.461
16.103
1.00
17.00


ATOM
884
N
TYR
A
179
7.354
61.917
19.665
1.00
24.20


ATOM
885
CA
TYR
A
179
8.454
62.076
20.615
1.00
17.23


ATOM
886
C
TYR
A
179
8.369
60.937
21.629
1.00
17.06


ATOM
887
O
TYR
A
179
9.362
60.267
21.913
1.00
16.76


ATOM
888
CB
TYR
A
179
8.364
53.410
21.359
1.00
21.87


ATOM
889
CG
TYR
A
179
9.236
63.440
22.595
1.00
22.98


ATOM
890
CD1
TYR
A
179
10.576
63.810
22.519
1.00
20.65


ATOM
891
CD2
TYR
A
179
8.738
63.025
23.830
1.00
22.75


ATOM
892
CE1
TYR
A
179
11.397
63.762
23.636
1.00
22.93


ATOM
893
CE2
TYR
A
179
9.552
62.974
24.951
1.00
28.14


ATOM
894
CZ
TYR
A
179
10.880
63.341
24.847
1.00
26.95


ATOM
895
OH
TYR
A
179
11.681
63.286
25.959
1.00
32.49


ATOM
896
N
LEU
A
180
7.170
60.712
22.162
1.00
16.69


ATOM
897
CA
LEU
A
180
6.963
59.660
23.149
1.00
18.83


ATOM
898
C
LEU
A
180
7.325
58.300
22.562
1.00
24.40


ATOM
899
O
LEU
A
180
8.024
57.498
23.192
1.00
26.33


ATOM
900
CB
LEU
A
180
5.501
59.657
23.629
1.00
21.53


ATOM
901
CG
LEU
A
180
5.032
60.716
24.644
1.00
21.20


ATOM
902
CD1
LEU
A
180
3.525
60.668
24.746
1.00
8.96


ATOM
903
CD2
LEU
A
180
5.652
60.458
26.013
1.00
15.59


ATOM
904
N
ARG
A
181
6.847
58.043
21.347
1.00
23.85


ATOM
905
CA
ARG
A
181
7.116
56.779
20.674
1.00
26.96


ATOM
906
C
ARG
A
181
8.600
56.613
20.284
1.00
29.51


ATOM
907
O
ARG
A
181
9.215
55.571
20.565
1.00
24.95


ATOM
908
CB
ARG
A
181
6.186
56.657
19.442
1.00
31.64


ATOM
909
CG
ARG
A
181
6.746
55.917
18.240
1.00
29.36


ATOM
910
CD
ARG
A
181
5.837
54.787
17.801
1.00
37.78


ATOM
911
NE
ARG
A
181
6.586
53.538
17.747
1.00
43.86


ATOM
912
CZ
ARG
A
181
6.895
52.800
18.811
1.00
47.64


ATOM
913
NH1
ARG
A
181
6.513
53.181
20.025
1.00
51.77


ATOM
914
NH2
ARG
A
181
7.623
51.702
18.666
1.00
48.00


ATOM
915
N
GLU
A
182
9.185
57.637
19.667
1.00
28.25


ATOM
916
CA
GLU
A
182
10.579
57.559
19.246
1.00
32.29


ATOM
917
C
GLU
A
182
11.579
57.667
20.403
1.00
36.52


ATOM
918
O
GLU
A
182
12.534
56.893
20.490
1.00
37.51


ATOM
919
CB
GLU
A
182
10.868
58.649
18.214
1.00
39.69


ATOM
920
CC
GLU
A
182
10.972
58.150
16.769
1.00
47.59


ATOM
921
CD
GLU
A
182
10.460
59.166
15.751
1.00
54.53


ATOM
922
OE1
GLU
A
182
9.533
58.821
14.981
1.00
59.11


ATOM
923
OE2
GLU
A
182
10.981
60.307
15.717
1.00
55.59


ATOM
924
N
LYS
A
183
11.354
58.617
21.302
1.00
34.85


ATOM
925
CA
LYS
A
183
12.267
58.802
22.410
1.00
31.76


ATOM
926
C
LYS
A
183
12.057
57.875
23.593
1.00
31.00


ATOM
927
O
LYS
A
183
12.998
57.601
24.324
1.00
34.57


ATOM
928
CB
LYS
A
183
12.205
60.253
22.875
1.00
31.46


ATOM
929
CG
LYS
A
183
12.649
61.239
21.807
1.00
34.29


ATOM
930
CD
LYS
A
183
13.908
60.759
21.095
1.00
38.20


ATOM
931
CE
LYS
A
183
14.730
61.922
20.559
1.00
38.45


ATOM
932
NZ
LYS
A
183
13.831
62.850
19.769
1.00
41.41


ATOM
933
N
HIS
A
184
10.844
57.373
23.734
1.00
33.70


ATOM
934
CA
HIS
A
184
10.577
56.498
24.926
1.00
29.58


ATOM
935
C
HIS
A
184
9.890
55.173
24.632
1.00
27.54


ATOM
936
O
HIS
A
184
9.577
54.378
25.483
1.00
23.78


ATOM
937
CB
HIS
A
184
9.790
57.288
25.976
1.00
29.02


ATOM
938
CG
HIS
A
184
10.494
58.533
26.420
1.00
31.48


ATOM
939
ND1
HIS
A
184
11.536
58.516
27.326
1.00
25.12


ATOM
940
CD2
HIS
A
184
10.379
59.818
26.001
1.00
30.21


ATOM
941
CE1
HIS
A
184
12.033
59.734
27.441
1.00
19.96


ATOM
942
NE2
HIS
A
184
11.351
60.544
26.648
1.00
19.98


ATOM
943
N
LYS
A
185
9.796
54.892
23.320
1.00
29.94


ATOM
944
CA
LYS
A
185
9.190
53.638
22.911
1.00
25.67


ATOM
945
C
LYS
A
185
7.890
53.334
23.628
1.00
23.62


ATOM
946
O
LYS
A
185
7.695
52.210
24.077
1.00
26.79


ATOM
947
CB
LYS
A
185
10.178
52.490
23.150
1.00
27.19


ATOM
948
CG
LYS
A
185
11.531
52.654
22.435
1.00
36.23


ATOM
949
CD
LYS
A
185
12.291
51.326
22.277
1.00
36.43


ATOM
950
CE
LYS
A
185
13.059
51.267
20.953
1.00
42.84


ATOM
951
NZ
LYS
A
185
14.269
52.150
20.924
1.00
41.69


ATOM
952
N
ILE
A
186
6.990
54.314
23.735
1.00
22.46


ATOM
953
CA
ILE
A
186
5.709
54.071
24.405
1.00
22.53


ATOM
954
C
ILE
A
186
4.540
54.777
23.720
1.00
23.99


ATOM
955
O
ILE
A
186
4.721
55.824
23.092
1.00
20.57


ATOM
956
CB
ILE
A
186
5.728
54.506
25.922
1.00
27.19


ATOM
957
CG1
ILE
A
186
5.423
56.001
26.070
1.00
24.94


ATOM
958
CG2
ILE
A
186
7.076
54.208
26.549
1.00
23.58


ATOM
959
CD1
ILE
A
186
6.433
56.898
25.415
1.00
28.89


ATOM
960
N
MET
A
187
3.348
54.187
23.825
1.00
20.86


ATOM
961
CA
MET
A
187
2.164
54.794
23.243
1.00
14.33


ATOM
962
C
MET
A
187
1.408
55.593
24.306
1.00
16.97


ATOM
963
O
MET
A
187
1.516
55.348
25.507
1.00
15.96


ATOM
964
CB
MET
A
187
1.247
53.727
22.617
1.00
18.58


ATOM
965
CG
MET
A
187
0.657
52.690
23.574
1.00
16.74


ATOM
966
SD
MET
A
187
−0.722
51.650
22.859
1.00
15.64


ATOM
967
CE
MET
A
187
−1.869
52.922
22.193
1.00
1.00


ATOM
968
N
HIS
A
188
0.644
86.569
23.870
1.00
14.62


ATOM
969
CA
HIS
A
188
−0.097
57.369
24.809
1.00
10.78


ATOM
970
C
HIS
A
188
−1.138
56.519
25.529
1.00
13.41


ATOM
971
O
HIS
A
188
−1.022
56.252
26.727
1.00
12.76


ATOM
972
CB
HIS
A
188
−0.761
58.509
24.072
1.00
7.01


ATOM
973
CG
HIS
A
188
−1.215
59.596
24.979
1.00
19.48


ATOM
974
NDI
HIS
A
188
−2.266
59.432
25.857
1.00
22.43


ATOM
975
CD2
HIS
A
188
−0.782
60.869
25.133
1.00
7.48


ATOM
976
CE1
HIS
A
188
−2.464
60.561
26.513
1.00
10.95


ATOM
977
NE2
HIS
A
188
−1.577
61.448
26.090
1.00
19.02


ATOM
978
N
ARG
A
189
−2.139
56.080
24.773
1.00
4.98


ATOM
979
CA
ARG
A
189
−3.205
55.231
25.259
1.00
1.00


ATOM
980
C
ARG
A
189
−4.383
55.951
25.774
1.00
1.00


ATOM
981
O
ARG
A
189
−5.309
55.310
26.213
1.00
−4.19


ATOM
982
CB
ARG
A
189
−2.720
54.284
26.337
1.00
1.00


ATOM
983
CG
ARG
A
189
−1.507
53.529
25.886
1.00
9.33


ATOM
984
CD
ARG
A
189
−0.859
52.801
27.025
1.00
21.68


ATOM
985
NE
ARG
A
189
−1.282
51.414
27.036
1.00
26.56


ATOM
986
CZ
ARG
A
189
−2.527
51.041
27.303
1.00
35.81


ATOM
987
NH1
ARG
A
189
−3.440
51.961
27.577
1.00
41.96


ATOM
988
NH2
ARG
A
189
−2.865
49.759
27.297
1.00
37.90


ATOM
989
N
ASP
A
190
−4.371
57.278
25.729
1.00
9.10


ATOM
990
CA
ASP
A
190
−5.516
58.024
26.248
1.00
6.50


ATOM
991
C
ASP
A
190
−5.598
59.437
25.699
1.00
7.95


ATOM
992
O
ASP
A
190
−5.799
60.392
26.448
1.00
11.22


ATOM
993
CB
ASP
A
190
−5.473
58.058
27.784
1.00
6.98


ATOM
994
CG
ASP
A
190
−6.825
58.454
28.419
1.00
15.04


ATOM
995
OD1
ASP
A
190
−7.874
58.430
27.731
1.00
17.20


ATOM
996
OD2
ASP
A
190
−6.835
58.796
29.629
1.00
22.60


ATOM
997
N
VAL
A
191
−5.454
59.581
24.386
1.00
6.04


ATOM
998
CA
VAL
A
191
−5.567
60.903
23.829
1.00
7.99


ATOM
999
C
VAL
A
191
−7.028
61.213
23.509
1.00
10.60


ATOM
1000
O
VAL
A
191
−7.794
60.371
23.158
1.00
16.67


ATOM
1001
CB
VAL
A
191
−4.729
61.088
22.524
1.00
7.90


ATOM
1002
CG1
VAL
A
191
−3.990
59.819
22.186
1.00
10.45


ATOM
1003
CG2
VAL
A
191
−5.596
61.587
21.389
1.00
8.16


ATOM
1004
N
LYS
A
192
−7.407
62.426
23.999
1.00
15.69


ATOM
1005
CA
LYS
A
192
−8.760
62.944
23.872
1.00
10.37


ATOM
1006
C
LYS
A
192
−8.635
64.404
24.241
1.00
13.21


ATOM
1007
O
LYS
A
192
−7.645
64.798
24.820
1.00
17.39


ATOM
1008
CB
LYS
A
192
−9.695
62.236
24.826
1.00
9.57


ATOM
1009
CG
LYS
A
192
−9.089
61.877
26.158
1.00
13.00


ATOM
1010
CD
LYS
A
192
−10.190
61.502
27.134
1.00
4.26


ATOM
1011
CE
LYS
A
192
−9.696
60.480
28.107
1.00
14.42


ATOM
1012
NZ
LYS
A
192
−10.306
60.658
29.454
1.00
14.54


ATOM
1013
N
PRO
A
193
−9.640
65.226
23.934
1.00
14.53


ATOM
1014
CA
PRO
A
193
−9.535
66.653
24.273
1.00
15.55


ATOM
1015
C
PRO
A
193
−9.030
67.005
25.691
1.00
21.41


ATOM
1016
O
PRO
A
193
−8.164
67.877
25.859
1.00
24.92


ATOM
1017
CB
PRO
A
193
−10.949
67.186
24.019
1.00
14.07


ATOM
1018
CG
PRO
A
193
−11.527
66.251
23.013
1.00
15.45


ATOM
1019
CD
PRO
A
193
−10.936
64.896
23.316
1.00
13.08


ATOM
1020
N
SER
A
194
−9.556
66.327
26.707
1.00
17.12


ATOM
1021
CA
SER
A
194
−9.170
66.619
28.084
1.00
11.99


ATOM
1022
C
SER
A
194
−7.722
66.313
28.462
1.00
12.87


ATOM
1023
O
SER
A
194
−7.259
66.758
29.512
1.00
15.78


ATOM
1024
CB
SER
A
194
−10.099
65.888
29.046
1.00
2.95


ATOM
1025
OG
SER
A
194
−9.735
64.525
29.109
1.00
4.10


ATOM
1026
N
ASN
A
195
−7.004
65.544
27.649
1.00
13.19


ATOM
1027
CA
ASN
A
195
−5.604
65.239
27.969
1.00
3.16


ATOM
1028
C
ASN
A
195
−4.659
65.979
27.033
1.00
3.51


ATOM
1029
O
ASN
A
195
−3.531
65.560
26.816
1.00
3.62


ATOM
1030
CB
ASN
A
195
−5.345
63.725
27.940
1.00
7.29


ATOM
1031
CG
ASN
A
195
−6.078
62.980
29.067
1.00
16.24


ATOM
1032
OD1
ASN
A
195
−6.705
63.609
29.918
1.00
22.53


ATOM
1033
ND2
ASN
A
195
−5.999
61.644
29.073
1.00
5.10


ATOM
1034
N
ILE
A
196
−5.144
67.078
26.462
1.00
10.19


ATOM
1035
CA
ILE
A
196
−4.345
67.935
25.587
1.00
11.06


ATOM
1036
C
ILE
A
196
−4.429
69.291
26.296
1.00
14.37


ATOM
1037
O
ILE
A
196
−5.478
69.943
26.302
1.00
11.81


ATOM
1038
CB
ILE
A
196
−4.951
68.067
24.159
1.00
8.54


ATOM
1039
CG1
ILE
A
196
−5.146
66.681
23.531
1.00
13.43


ATOM
1040
CG2
ILE
A
196
−4.049
68.920
23.284
1.00
3.89


ATOM
1041
CD1
ILE
A
196
−5.747
66.709
22.132
1.00
9.24


ATOM
1042
N
LEU
A
197
−3.331
69.706
26.909
1.00
13.27


ATOM
1043
CA
LEU
A
197
−3.327
70.961
27.645
1.00
18.16


ATOM
1044
C
LEU
A
197
−2.768
72.150
26.867
1.00
20.90


ATOM
1045
O
LEU
A
197
−1.782
72.028
26.140
1.00
24.12


ATOM
1046
CB
LEU
A
197
−2.537
70.767
28.931
1.00
9.76


ATOM
1047
CG
LEU
A
197
−3.316
70.231
30.123
1.00
14.11


ATOM
1048
CD1
LEU
A
197
−4.468
69.396
29.668
1.00
10.30


ATOM
1049
CD2
LEU
A
197
−2.391
69.432
31.006
1.00
15.62


ATOM
1050
N
VAL
A
198
−3.422
73.298
26.996
1.00
19.80


ATOM
1051
CA
VAL
A
198
−2.937
74.503
26.328
1.00
25.06


ATOM
1052
C
VAL
A
198
−2.563
75.594
27.362
1.00
25.90


ATOM
1053
O
VAL
A
198
−2.758
75.414
28.566
1.00
22.42


ATOM
1054
CB
VAL
A
198
−3.986
75.061
25.333
1.00
23.02


ATOM
1055
CC1
VAL
A
198
−4.088
74.141
24.130
1.00
25.99


ATOM
1056
CG2
VAL
A
198
−5.334
75.205
26.008
1.00
26.53


ATOM
1057
N
ASN
A
199
−1.993
76.703
26.891
1.00
26.25


ATOM
1058
CA
ASN
A
199
−1.515
77.796
27.779
1.00
23.88


ATOM
1059
C
ASN
A
199
−1.535
79.153
27.075
1.00
29.40


ATOM
1060
O
ASN
A
199
−1.406
79.232
25.853
1.00
24.22


ATOM
1061
CB
ASN
A
199
−0.307
77.452
28.521
1.00
9.76


ATOM
1062
CG
ASN
A
199
0.943
77.663
27.675
1.00
16.12


ATOM
1063
OD1
ASN
A
199
2.027
77.204
28.050
1.00
16.82


ATOM
1064
ND2
ASN
A
199
0.812
78.347
26.550
1.00
10.04


ATOM
1065
N
SER
A
200
−1.632
80.219
27.863
1.00
36.99


ATOM
1066
CA
SER
A
200
−1.614
81.589
27.350
1.00
40.77


ATOM
1067
C
SER
A
200
−0.458
81.877
26.401
1.00
42.42


ATOM
1068
O
SER
A
200
−0.506
82.810
25.607
1.00
43.48


ATOM
1069
CB
SER
A
200
−1.549
62.561
28.516
1.00
36.57


ATOM
1070
OG
SER
A
200
−0.511
82.174
29.392
1.00
40.92


ATOM
1071
N
ARG
A
201
0.820
81.208
26.398
1.00
44.32


ATOM
1072
CA
ARG
A
201
1.988
81.346
25.549
1.00
43.41


ATOM
1073
C
ARG
A
201
1.780
80.725
24.177
1.00
43.74


ATOM
1074
O
ARG
A
201
2.651
80.815
23.320
1.00
48.13


ATOM
1075
CB
ARG
A
201
3.179
80.702
26.243
1.00
46.39


ATOM
1076
CG
ARG
A
201
2.972
80.550
27.745
1.00
55.29


ATOM
1077
CD
ARG
A
201
4.271
80.726
28.488
1.00
62.48


ATOM
1078
NE
ARG
A
201
5.353
79.986
27.845
1.00
69.50


ATOM
1079
CZ
ARG
A
201
5.844
78.841
28.305
1.00
75.38


ATOM
1080
NH1
ARG
A
201
5.351
78.299
29.415
1.00
76.77


ATOM
1081
NH2
ARG
A
201
6.829
78.233
27.650
1.00
76.77


ATOM
1082
N
GLY
A
202
0.626
80.101
23.961
1.00
41.65


ATOM
1083
CA
GLY
A
202
0.354
79.486
22.671
1.00
39.21


ATOM
1084
C
GLY
A
202
0.821
78.044
22.571
1.00
34.48


ATOM
1085
O
GLY
A
202
0.775
77.431
21.503
1.00
27.95


ATOM
1086
N
GLU
A
203
1.265
77.505
23.701
1.00
34.61


ATOM
1087
CA
GLU
A
203
1.747
76.135
23.770
1.00
34.41


ATOM
1088
C
GLU
A
203
0.594
75.115
23.869
1.00
32.38


ATOM
1089
O
GLU
A
203
−0.457
75.378
24.456
1.00
29.49


ATOM
1090
CB
GLU
A
203
2.704
75.988
24.958
1.00
35.99


ATOM
1091
CG
GLU
A
203
4.163
76.308
24.637
1.00
38.65


ATOM
1092
CD
GLU
A
203
5.065
76.247
25.861
1.00
42.02


ATOM
1093
OE1
GLU
A
203
4.638
76.717
26.934
1.00
42.72


ATOM
1094
OE2
GLU
A
203
6.199
75.726
25.753
1.00
44.37


ATOM
1095
N
ILE
A
204
0.812
73.948
23.277
1.00
29.50


ATOM
1096
CA
ILE
A
204
−0.184
72.884
23.264
1.00
23.36


ATOM
1097
C
ILE
A
204
0.547
71.620
23.637
1.00
19.48


ATOM
1098
O
ILE
A
204
1.433
71.190
22.908
1.00
18.22


ATOM
1099
CB
ILE
A
204
−0.775
72.725
21.860
1.00
21.23


ATOM
1100
CC1
ILE
A
204
−1.297
74.079
21.361
1.00
20.55


ATOM
1101
CG2
ILE
A
204
−1.867
71.682
21.884
1.00
24.25


ATOM
1102
CD1
ILE
A
204
−1.979
74.031
19.991
1.00
23.30


ATOM
1103
N
LYS
A
205
0.183
71.020
24.767
1.00
17.60


ATOM
1104
CA
LYS
A
205
0.868
69.820
25.222
1.00
13.58


ATOM
1105
C
LYS
A
205
−0.050
68.694
25.632
1.00
9.43


ATOM
1106
O
LYS
A
205
−1.233
68.897
25.893
1.00
11.03


ATOM
1107
CB
LYS
A
205
1.787
70.153
26.395
1.00
20.21


ATOM
1108
CG
LYS
A
205
2.519
71.481
26.251
1.00
22.19


ATOM
1109
CD
LYS
A
205
3.617
71.618
27.318
1.00
28.07


ATOM
1110
CE
LYS
A
205
4.629
72.702
26.942
1.00
24.19


ATOM
1111
NZ
LYS
A
205
5.301
73.302
28.125
1.00
24.47


ATOM
1112
N
LEU
A
206
0.231
67.507
25.732
1.00
6.38


ATOM
1113
CA
LEU
A
206
−0.197
66.301
26.104
1.00
10.11


ATOM
1114
C
LEU
A
206
0.141
65.877
27.513
1.00
9.98


ATOM
1115
O
LEU
A
206
1.305
65.915
27.915
1.00
11.25


ATOM
1116
CB
LEU
A
206
0.201
65.124
25.193
1.00
11.39


ATOM
1117
CG
LEU
A
206
−0.442
64.733
23.867
1.00
7.60


ATOM
1118
CD1
LEU
A
206
−1.260
65.827
23.278
1.00
11.01


ATOM
1119
CD2
LEU
A
206
0.655
64.373
22.941
1.00
1.68


ATOM
1120
N
CYS
A
206
−0.865
65.425
28.245
1.00
4.73


ATOM
1121
CA
CYS
A
207
−0.651
64.913
29.589
1.00
8.41


ATOM
1122
C
CYS
A
207
−1.366
63.578
29.682
1.00
13.52


ATOM
1123
O
CYS
A
207
−1.968
63.105
28.719
1.00
10.76


ATOM
1124
CB
CYS
A
207
−1.267
65.835
30.630
1.00
6.53


ATOM
1125
SG
CYS
A
207
−3.024
66.080
30.340
1.00
13.39


ATOM
1126
N
ASP
A
208
−1.294
62.982
30.861
1.00
15.78


ATOM
1127
CA
ASP
A
208
−1.973
61.736
31.143
1.00
17.32


ATOM
1128
C
ASP
A
208
−1.711
60.540
30.221
1.00
18.84


ATOM
1129
O
ASP
A
208
−2.647
59.806
29.899
1.00
18.11


ATOM
1130
CB
ASP
A
208
−3.481
62.003
31.206
1.00
18.66


ATOM
1131
CG
ASP
A
208
−3.873
62.871
32.385
1.00
22.68


ATOM
1132
OD1
ASP
A
208
−4.998
63.396
32.385
1.00
20.44


ATOM
1133
OD2
ASP
A
208
−3.061
63.032
33.315
1.00
26.55


ATOM
1134
N
PHE
A
209
−0.467
60.329
29.800
1.00
14.63


ATOM
1135
CA
PHE
A
209
−0.176
59.176
28.966
1.00
18.87


ATOM
1136
C
PHE
A
209
0.212
58.018
29.867
1.00
20.60


ATOM
1137
O
PHE
A
209
0.407
58.214
31.054
1.00
20.15


ATOM
1138
CB
PHE
A
209
0.926
59.465
27.953
1.00
17.74


ATOM
1139
CG
PHE
A
209
1.998
60.365
28.454
1.00
12.99


ATOM
1140
CD1
PHE
A
209
1.873
61.744
28.322
1.00
17.78


ATOM
1141
CD2
PHE
A
209
3.172
59.837
28.968
1.00
7.67


ATOM
1142
CE1
PHE
A
209
2.907
62.587
28.690
1.00
13.83


ATOM
1143
CE2
PHE
A
209
4.196
60.633
29.299
1.00
9.69


ATOM
1144
CZ
PHE
A
209
4.079
62.042
29.196
1.00
14.31


ATOM
1145
N
GLY
A
210
0.330
56.819
29.301
1.00
19.53


ATOM
1146
CA
GLY
A
210
0.635
55.646
30.098
1.00
17.23


ATOM
1147
C
GLY
A
210
2.088
55.267
30.263
1.00
23.73


ATOM
1148
O
GLY
A
210
2.583
54.390
29.546
1.00
23.36


ATOM
1149
N
VAL
A
211
2.766
55.903
31.222
1.00
18.69


ATOM
1150
CA
VAL
A
211
4.175
55.624
31.486
1.00
15.92


ATOM
1151
C
VAL
A
211
4.343
54.460
32.456
1.00
18.33


ATOM
1152
O
VAL
A
211
5.406
53.844
32.513
1.00
23.10


ATOM
1153
CB
VAL
A
211
4.919
56.853
32.099
1.00
15.49


ATOM
1154
CG1
VAL
A
211
5.258
57.856
31.015
1.00
20.17


ATOM
1155
CG2
VAL
A
211
4.057
57.515
33.182
1.00
8.13


ATOM
1156
N
SER
A
212
3.300
54.158
33.219
1.00
16.14


ATOM
1157
CA
SER
A
212
3.400
53.084
34.192
1.00
16.89


ATOM
1158
C
SER
A
212
2.437
51.933
33.950
1.00
17.75


ATOM
1159
O
SER
A
212
1.210
52.084
34.035
1.00
11.52


ATOM
1160
CB
SER
A
212
3.200
53.645
35.612
1.00
22.55


ATOM
1161
OG
SER
A
212
2.661
52.692
36.524
1.00
14.76


ATOM
1162
N
GLY
A
213
3.002
50.772
33.650
1.00
18.52


ATOM
1163
CA
GLY
A
213
2.169
49.612
33.430
1.00
22.77


ATOM
1164
C
GLY
A
213
1.353
49.343
34.678
1.00
22.25


ATOM
1165
O
GLY
A
213
0.155
49.041
34.611
1.00
20.29


ATOM
1166
N
GLN
A
214
2.015
49.465
35.826
1.00
27.41


ATOM
1167
CA
GLN
A
214
1.371
49.232
37.114
1.00
25.26


ATOM
1168
C
GLN
A
214
0.242
50.229
37.331
1.00
24.17


ATOM
1169
O
GLN
A
214
−0.783
49.887
37.920
1.00
24.74


ATOM
1170
CB
GLN
A
214
2.390
49.334
38.240
1.00
30.54


ATOM
1171
CG
GLN
A
214
2.430
48.128
39.161
1.00
32.29


ATOM
1172
CD
GLN
A
214
1.068
47.495
39.317
1.00
36.82


ATOM
1173
OE1
GLN
A
214
0.067
40.190
39.500
1.00
39.11


ATOM
1174
NE2
GLN
A
214
1.016
46.172
39.239
1.00
34.02


ATOM
1175
N
LEU
A
215
0.421
51.462
36.859
1.00
21.87


ATOM
1176
CA
LEU
A
215
−0.637
82.447
37.013
1.00
22.64


ATOM
1177
C
LEU
A
215
−1.792
52.021
36.112
1.00
25.00


ATOM
1178
O
LEU
A
215
−2.929
51.900
36.578
1.00
23.14


ATOM
1179
CB
LEU
A
215
−0.153
53.856
36.644
1.00
21.78


ATOM
1180
CG
LEU
A
215
−1.039
54.950
37.248
1.00
22.99


ATOM
1181
CD1
LEU
A
215
−1.500
54.507
38.630
1.00
12.37


ATOM
1182
CD2
LEU
A
215
−0.285
56.257
37.339
1.00
21.05


ATOM
1183
N
ILE
A
216
−1.489
51.766
34.833
1.00
25.13


ATOM
1184
CA
ILE
A
216
−2.498
51.314
33.868
1.00
26.43


ATOM
1185
C
ILE
A
216
−3.306
50.177
34.522
1.00
29.08


ATOM
1186
O
ILE
A
216
−4.545
50.203
34.563
1.00
25.25


ATOM
1187
CB
ILE
A
216
−1.846
50.754
32.572
1.00
24.55


ATOM
1188
CG1
ILE
A
216
−1.290
51.881
31.711
1.00
17.39


ATOM
1189
CG2
ILE
A
216
−2.887
50.022
31.739
1.00
24.26


ATOM
1190
CD1
ILE
A
216
−0.088
51.464
30.873
1.00
17.82


ATOM
1191
N
ASP
A
217
−2.589
49.184
35.034
1.00
31.63


ATOM
1192
CA
ASP
A
217
−3.222
48.049
35.684
1.00
37.82


ATOM
1193
C
ASP
A
217
−4.168
48.528
36.771
1.00
38.70


ATOM
1194
O
ASP
A
217
−5.383
48.396
36.642
1.00
36.98


ATOM
1195
CB
ASP
A
217
−2.161
47.129
36.295
1.00
46.25


ATOM
1196
CG
ASP
A
217
−1.600
46.139
35.289
1.00
56.08


ATOM
1197
OD1
ASP
A
217
−1.754
46.378
34.069
1.00
69.08


ATOM
1198
OD2
ASP
A
217
−1.004
45.121
35.715
1.00
60.98


ATOM
1199
N
SER
A
218
−3.608
49.104
37.829
1.00
38.42


ATOM
1200
CA
SER
A
218
−4.410
49.579
38.947
1.00
39.52


ATOM
1201
C
SER
A
218
−5.500
50.553
38.578
1.00
41.42


ATOM
1202
O
SER
A
218
−6.219
51.038
39.448
1.00
44.53


ATOM
1203
CB
SER
A
218
−3.510
50.197
40.009
1.00
37.46


ATOM
1204
OG
SER
A
218
−2.555
49.248
40.430
1.00
39.57


ATOM
1205
N
MET
A
219
−5.651
50.863
37.302
1.00
46.31


ATOM
1206
CA
MET
A
219
−6.719
51.762
36.896
1.00
53.76


ATOM
1207
C
MET
A
219
−7.731
50.953
36.082
1.00
56.84


ATOM
1208
O
MET
A
219
−8.157
51.363
35.003
1.00
60.21


ATOM
1209
CB
MET
A
219
−6.165
52.931
36.068
1.00
54.06


ATOM
1210
CG
MET
A
219
−4.905
53.579
36.640
1.00
55.99


ATOM
1211
SD
MET
A
219
−5.081
55.303
37.181
1.00
54.86


ATOM
1212
CE
MET
A
219
−6.131
55.068
38.631
1.00
46.80


ATOM
1213
N
ALA
A
220
−8.109
49.797
36.621
1.00
59.86


ATOM
1214
CA
ALA
A
220
−9.065
48.898
35.974
1.00
59.07


ATOM
1215
C
ALA
A
220
−10.476
49.481
35.913
1.00
59.01


ATOM
1216
O
ALA
A
220
−11.106
49.486
34.852
1.00
55.25


ATOM
1217
CB
ALA
A
220
−9.093
47.561
36.710
1.00
57.22


ATOM
1218
N
ASN
A
221
−10.960
49.974
37.052
1.00
60.48


ATOM
1219
CA
ASN
A
221
−12.304
50.549
37.160
1.00
60.01


ATOM
1220
C
ASN
A
221
−12.365
52.068
36.929
1.00
57.20


ATOM
1221
O
ASN
A
221
−13.283
52.510
36.208
1.00
53.31


ATOM
1222
CB
ASN
A
221
−12.503
50.210
38.537
1.00
59.42


ATOM
1223
CG
ASN
A
221
−12.642
48.769
38.959
1.00
61.87


ATOM
1224
OD1
ASN
A
221
−11.650
48.144
38.557
1.00
58.70


ATOM
1225
ND2
ASN
A
221
−13.541
48.213
39.778
1.00
63.04


ATOM
1226
N
SER
A
222
−11.346
53.157
37.210
1.00
57.70


ATOM
1227
N
VAL
A
224
−13.882
55.228
31.393
1.00
73.05


ATOM
1228
CA
VAL
A
224
−14.409
56.543
30.920
1.00
72.43


ATOM
1229
C
VAL
A
224
−15.906
56.404
30.663
1.00
70.78


ATOM
1230
O
VAL
A
224
−16.410
55.290
30.519
1.00
72.56


ATOM
1231
CB
VAL
A
224
−13.669
57.005
29.618
1.00
73.49


ATOM
1232
CG1
VAL
A
224
−14.604
57.795
28.695
1.00
75.72


ATOM
1233
CG2
VAL
A
224
−12.467
57.858
29.939
1.00
71.02


ATOM
1234
N
GLY
A
225
−16.616
57.528
30.626
1.00
69.28


ATOM
1235
CA
GLY
A
225
−18.049
57.488
30.390
1.00
66.97


ATOM
1236
C
CLY
A
225
−18.405
56.922
29.026
1.00
64.94


ATOM
1237
O
GLY
A
225
−17.548
55.342
28.352
1.00
64.02


ATOM
1238
N
THR
A
226
−19.672
57.081
28.631
1.00
61.39


ATOM
1239
CA
THR
A
226
−20.161
56.607
27.336
1.00
54.72


ATOM
1240
C
THR
A
226
−19.181
57.006
26.229
1.00
52.97


ATOM
1241
O
THR
A
226
−18.343
56.206
25.810
1.00
55.32


ATOM
1242
CB
THR
A
226
−21.538
57.220
26.997
1.00
55.83


ATOM
1243
OG1
THR
A
226
−22.116
57.775
28.181
1.00
49.67


ATOM
1244
CG2
THR
A
226
−22.479
56.156
26.403
1.00
53.80


ATOM
1245
N
ARG
A
227
−19.292
58.244
25.757
1.00
43.94


ATOM
1246
CA
ARG
A
227
−18.407
58.742
24.714
1.00
40.03


ATOM
1247
C
ARG
A
227
−16.984
58.165
24.837
1.00
37.22


ATOM
1248
O
ARG
A
227
−16.214
58.556
25.720
1.00
42.82


ATOM
1249
CB
ARG
A
227
−18.379
60.271
24.773
1.00
39.52


ATOM
1250
CG
ARG
A
227
−19.773
60.891
24.751
1.00
46.07


ATOM
1251
CD
ARG
A
227
−19.882
62.091
25.679
1.00
52.06


ATOM
1252
NE
ARG
A
227
−19.849
63.357
24.949
1.00
53.53


ATOM
1253
CZ
ARG
A
227
−18.736
63.935
24.500
1.00
53.26


ATOM
1254
NH1
ARG
A
227
−17.558
63.359
24.704
1.00
54.16


ATOM
1255
NH2
ARG
A
227
−18.797
65.091
23.845
1.00
48.57


ATOM
1256
N
SER
A
228
−16.650
57.224
23.955
1.00
27.69


ATOM
1257
CA
SER
A
228
−15.331
56.588
23.946
1.00
21.04


ATOM
1258
C
SER
A
228
−14.465
57.083
22.791
1.00
17.51


ATOM
1259
O
SER
A
228
−14.970
57.453
21.740
1.00
18.61


ATOM
1260
CB
SER
A
228
−15.471
55.068
23.847
1.00
16.43


ATOM
1261
OG
SER
A
228
−14.236
54.432
24.114
1.00
17.59


ATOM
1252
N
TYR
A
229
−13.155
57.111
22.996
1.00
18.98


ATOM
1263
CA
TYR
A
229
−12.232
57.543
21.958
1.00
11.61


ATOM
1264
C
TYR
A
229
−11.298
56.380
21.727
1.00
9.85


ATOM
1265
O
TYR
A
229
−10.280
56.509
21.038
1.00
9.69


ATOM
1266
CB
TYR
A
229
−11.442
58.785
22.382
1.00
8.85


ATOM
1267
CG
TYR
A
229
−12.297
60.018
22.551
1.00
7.07


ATOM
1268
CD1
TYR
A
229
−12.462
60.926
21.518
1.00
6.82


ATOM
1269
CD2
TYR
A
229
−13.001
60.236
23.734
1.00
10.05


ATOM
1270
CE1
TYR
A
229
−13.321
62.022
21.652
1.00
11.84


ATOM
1271
CE2
TYR
A
229
−13.854
61.317
23.879
1.00
3.10


ATOM
1272
CZ
TYR
A
229
−14.016
62.200
22.836
1.00
10.50


ATOM
1273
OH
TYR
A
229
−14.917
63.224
22.974
1.00
13.64


ATOM
1274
N
MET
A
230
−11.652
55.243
22.322
1.00
4.53


ATOM
1275
CA
MET
A
230
−10.872
54.024
22.161
1.00
11.52


ATOM
1276
C
MET
A
230
−10.972
53.492
20.719
1.00
14.18


ATOM
1277
O
MET
A
230
−12.027
53.543
20.085
1.00
5.79


ATOM
1278
CB
MET
A
230
−11.381
52.934
23.081
1.00
18.26


ATOM
1279
CG
MET
A
230
−11.524
53.332
24.503
1.00
18.76


ATOM
1280
SD
MET
A
230
−10.711
52.093
25.469
1.00
27.82


ATOM
1281
CE
MET
A
230
−11.466
52.424
27.070
1.00
34.63


ATOM
1282
N
SER
A
231
−9.863
52.970
20.220
1.00
11.84


ATOM
1283
CA
SER
A
231
−9.836
52.429
18.881
1.00
13.96


ATOM
1284
C
SER
A
231
−10.596
51.103
18.888
1.00
16.30


ATOM
1285
O
SER
A
231
−10.750
50.447
19.936
1.00
14.37


ATOM
1286
CB
SER
A
231
−8.288
52.206
18.418
1.00
5.81


ATOM
1287
OG
SER
A
231
−7.869
51.006
18.960
1.00
5.77


ATOM
1288
N
PRO
A
232
−11.103
50.702
17.713
1.00
16.03


ATOM
1289
CA
PRO
A
232
−11.848
49.445
17.589
1.00
12.50


ATOM
1290
C
PRO
A
232
−11.026
48.273
18.094
1.00
9.49


ATOM
1291
O
PRO
A
232
−11.552
47.398
18.792
1.00
9.39


ATOM
1292
CB
PRO
A
232
−12.141
49.342
16.101
1.00
16.44


ATOM
1293
CG
PRO
A
232
−12.076
50.748
15.609
1.00
17.49


ATOM
1294
CD
PRO
A
232
−11.024
51.424
16.434
1.00
16.19


ATOM
1295
N
GLU
A
233
−9.735
48.261
17.764
1.00
2.58


ATOM
1296
CA
GLU
A
233
−8.883
47.159
18.219
1.00
8.07


ATOM
1297
C
GLU
A
233
−8.755
47.165
19.743
1.00
12.93


ATOM
1298
O
GLU
A
233
−8.970
45.132
20.392
1.00
12.72


ATOM
1299
CB
GLU
A
233
−7.493
47.189
17.529
1.00
4.71


ATOM
1300
CG
GLU
A
233
−6.558
48.318
17.909
1.00
12.03


ATOM
1301
CD
GLU
A
233
−6.659
49.492
16.955
1.00
22.82


ATOM
1302
OE1
GLU
A
233
−5.684
50.291
16.928
1.00
11.37


ATOM
1303
OE2
GLU
A
233
−7.709
49.613
16.247
1.00
10.91


ATOM
1304
N
ARG
A
234
−8.434
48.329
20.318
1.00
13.03


ATOM
1305
CA
ARG
A
234
−8.324
48.431
21.770
1.00
7.45


ATOM
1306
C
ARG
A
234
−9.634
48.001
22.401
1.00
3.63


ATOM
1307
O
ARG
A
234
−9.630
47.249
23.365
1.00
7.47


ATOM
1308
CB
ARG
A
234
−7.995
49.854
22.206
1.00
9.92


ATOM
1309
CG
ARG
A
234
−7.295
49.906
23.547
1.00
15.19


ATOM
1310
CD
ARG
A
234
−7.151
51.322
24.072
1.00
12.50


ATOM
1311
NE
ARG
A
234
−7.161
51.313
25.523
1.00
25.86


ATOM
1312
CZ
ARG
A
234
−6.578
52.219
26.299
1.00
20.07


ATOM
1313
NH1
ARG
A
234
−5.916
53.247
25.779
1.00
13.56


ATOM
1314
NH2
ARG
A
234
−6.646
52.065
27.607
1.00
12.50


ATOM
1315
N
LEU
A
235
−10.757
48.463
21.850
1.00
1.00


ATOM
1316
CA
LEU
A
235
−12.067
48.088
22.378
1.00
6.12


ATOM
1317
C
LEU
A
235
−12.322
46.567
22.351
1.00
13.38


ATOM
1318
O
LEU
A
235
−13.054
46.039
23.189
1.00
15.84


ATOM
1319
CB
LEU
A
235
−13.166
48.769
21.574
1.00
2.62


ATOM
1320
CG
LEU
A
235
−13.538
50.230
21.800
1.00
14.11


ATOM
1321
CD1
LEU
A
235
−14.914
50.460
21.213
1.00
5.49


ATOM
1322
CD2
LEU
A
235
−13.541
50.573
23.291
1.00
11.85


ATOM
1323
N
GLN
A
236
−11.710
45.858
21.401
1.00
15.05


ATOM
1324
CA
GLN
A
236
−11.946
44.423
21.280
1.00
17.07


ATOM
1325
C
GLN
A
236
−10.961
43.478
21.983
1.00
16.84


ATOM
1226
O
GLN
A
236
−11.325
42.358
22.354
1.00
19.39


ATOM
1327
CB
GLN
A
236
−12.082
44.056
19.790
1.00
18.30


ATOM
1328
CG
GLN
A
236
−13.448
44.464
19.201
1.00
22.72


ATOM
1329
CD
GLN
A
236
−13.455
44.652
17.670
1.00
31.91


ATOM
1330
OE1
GLN
A
236
−12.406
44.778
17.033
1.00
25.55


ATOM
1331
NE2
GLN
A
236
−14.655
44.681
17.085
1.00
32.13


ATOM
1332
N
GLY
A
237
−9.722
43.900
22.186
1.00
13.06


ATOM
1333
CA
GLY
A
237
−8.807
43.002
22.864
1.00
12.96


ATOM
1334
C
GLY
A
237
−7.502
43.648
23.260
1.00
18.20


ATOM
1335
O
GLY
A
237
−0.418
44.856
23.416
1.00
18.82


ATOM
1336
N
THR
A
238
−6.483
42.814
23.409
1.00
24.69


ATOM
1337
CA
THR
A
238
−5.136
43.229
23.786
1.00
27.84


ATOM
1338
C
THR
A
238
−4.254
43.518
22.562
1.00
28.84


ATOM
1339
O
THR
A
238
−3.078
43.865
22.703
1.00
29.67


ATOM
1340
CB
THR
A
238
−4.435
42.101
24.580
1.00
31.65


ATOM
1341
OG1
THR
A
238
−4.049
41.060
23.667
1.00
36.43


ATOM
1342
CG2
THR
A
238
−5.370
41.497
25.630
1.00
29.39


ATOM
1343
N
HIS
A
239
−4.798
43.360
21.362
1.00
28.94


ATOM
1344
CA
HIS
A
239
−3.986
43.584
20.174
1.00
29.55


ATOM
1345
C
HIS
A
239
−4.077
44.996
19.628
1.00
28.05


ATOM
1346
O
HIS
A
239
−4.747
45.263
18.620
1.00
29.66


ATOM
1347
CB
HIS
A
239
−4.335
42.568
19.086
1.00
30.81


ATOM
1348
CG
HIS
A
239
−4.002
41.156
19.459
1.00
33.94


ATOM
1349
ND1
HIS
A
239
−4.953
40.251
19.881
1.00
36.18


ATOM
1350
CD2
HIS
A
239
−2.798
40.499
19.503
1.00
34.71


ATOM
1351
CE1
HIS
A
239
−4.369
39.103
20.174
1.00
32.97


ATOM
1252
NE2
HIS
A
239
−3.072
39.229
19.956
1.00
36.62


ATOM
1353
N
TYR
A
240
−2.391
45.896
20.318
1.00
22.57


ATOM
1354
CA
TYR
A
240
−3.336
47.286
19.923
1.00
20.14


ATOM
1355
C
TYR
A
240
−2.040
47.844
20.482
1.00
19.73


ATOM
1356
O
TYR
A
240
−1.405
47.222
21.346
1.00
15.28


ATOM
1357
CB
TYR
A
240
−4.622
48.056
20.493
1.00
24.44


ATOM
1358
CG
TYR
A
240
−4.408
48.269
21.976
1.00
31.08


ATOM
1359
CD1
TYR
A
240
−3.992
49.498
22.496
1.00
33.64


ATOM
1360
CD2
TYR
A
240
−4.663
47.228
22.862
1.00
31.36


ATOM
1361
CE1
TYR
A
240
−3.820
49.684
22.865
1.00
28.24


ATOM
1362
CE2
TYR
A
240
−4.508
47.396
24.226
1.00
32.79


ATOM
1363
CZ
TYR
A
240
−4.087
48.627
24.720
1.00
33.22


ATOM
1364
OH
TYR
A
240
−3.907
48.777
26.067
1.00
33.85


ATOM
1365
N
SER
A
241
−1.647
49.010
19.975
1.00
14.20


ATOM
1366
CA
SER
A
241
−0.442
49.690
20.412
1.00
6.35


ATOM
1367
C
SER
A
241
−0.506
51.170
20.021
1.00
2.08


ATOM
1268
O
SER
A
241
−1.582
51.772
20.056
1.00
2.96


ATOM
1369
CB
SER
A
241
0.786
49.017
19.802
1.00
11.60


ATOM
1370
OG
SER
A
241
1.960
49.780
20.037
1.00
21.68


ATOM
1371
N
VAL
A
242
0.278
51.587
18.833
1.00
2.29


ATOM
1372
CA
VAL
A
242
0.391
53.025
18.606
1.00
8.94


ATOM
1373
C
VAL
A
242
−0.536
53.651
17.571
1.00
15.31


ATOM
1374
O
VAL
A
242
−0.836
54.856
17.648
1.00
15.12


ATOM
1375
CB
VAL
A
242
1.825
53.392
18.259
1.00
17.11


ATOM
1376
CG1
VAL
A
242
2.758
52.850
19.332
1.00
16.09


ATOM
1377
CG2
VAL
A
242
2.178
52.831
16.894
1.00
17.52


ATOM
1378
N
GLN
A
243
−0.978
52.853
16.597
1.00
13.56


ATOM
1379
CA
GLN
A
243
−1.889
53.342
15.570
1.00
6.91


ATOM
1380
C
GLN
A
243
−3.189
53.776
16.236
1.00
4.90


ATOM
1381
O
GLN
A
243
−3.867
54.686
15.770
1.00
13.17


ATOM
1382
CB
GLN
A
243
−2.183
52.231
14.547
1.00
18.34


ATOM
1383
CG
GLN
A
243
−1.292
52.227
13.298
1.00
13.69


ATOM
1384
CD
GLN
A
243
−1.018
53.611
12.756
1.00
15.91


ATOM
1385
OE1
GLN
A
243
−0.023
54.285
13.203
1.00
21.34


ATOM
1386
NE2
GLN
A
243
−1.877
54.086
11.858
1.00
20.85


ATOM
1387
N
SEP
A
244
−3.551
53.096
17.320
1.00
6.15


ATOM
1388
CA
SER
A
244
−4.763
53.412
18.071
1.00
4.95


ATOM
1389
C
SER
A
244
−4.849
54.887
18.527
1.00
10.20


ATOM
1390
O
SER
A
244
−5.952
55.438
18.667
1.00
11.43


ATOM
1391
CB
SER
A
244
−4.860
52.501
19.279
1.00
3.14


ATOM
1392
OG
SER
A
244
−6.182
52.510
19.770
1.00
18.08


ATOM
1393
N
ASP
A
245
−2.690
55.524
18.739
1.00
8.16


ATOM
1394
CA
ASP
A
245
−3.659
56.919
19.157
1.00
12.93


ATOM
1395
C
ASP
A
245
−4.115
57.826
18.016
1.00
18.15


ATOM
1396
O
ASP
A
245
−4.715
58.891
18.258
1.00
18.63


ATOM
1397
CB
ASP
A
245
−2.241
57.347
19.593
1.00
16.81


ATOM
1398
CG
ASP
A
245
−1.808
56.758
20.951
1.00
16.67


ATOM
1399
OD1
ASP
A
245
−0.587
56.538
21.121
1.00
11.97


ATOM
1400
OD2
ASP
A
245
−2.666
56.509
21.839
1.00
12.98


ATOM
1401
N
ILE
A
246
−3.836
57.408
16.775
1.00
17.55


ATOM
1402
CA
ILE
A
246
−4.209
58.204
15.604
1.00
13.94


ATOM
1403
C
ILE
A
246
−5.709
58.355
15.511
1.00
11.92


ATOM
1404
O
ILE
A
246
−6.208
59.454
15.236
1.00
10.02


ATOM
1405
CB
ILE
A
246
−3.690
57.585
14.266
1.00
19.52


ATOM
1406
CG1
ILE
A
246
−2.165
57.550
14.269
1.00
13.12


ATOM
1407
CD2
ILE
A
246
−4.169
58.434
13.065
1.00
13.77


ATOM
1408
CD1
ILE
A
246
−1.539
58.911
14.456
1.00
17.58


ATOM
1409
N
TRP
A
247
−5.426
57.254
15.737
1.00
15.90


ATOM
1410
CA
TRP
A
247
−7.893
57.272
15.685
1.00
15.15


ATOM
1411
C
TRP
A
247
−8.416
58.300
16.712
1.00
17.52


ATOM
1412
O
TRP
A
247
−9.204
59.214
16.374
1.00
11.79


ATOM
1413
CB
TRP
A
247
−8.455
55.864
15.988
1.00
14.62


ATOM
1414
CG
TRP
A
247
−9.951
55.839
16.231
1.00
17.81


ATOM
1415
CD1
TRP
A
247
−10.506
56.140
17.398
1.00
21.33


ATOM
1416
CD2
TRP
A
247
−10.969
55.581
15.261
1.00
24.47


ATOM
1417
NE1
TRP
A
247
−11.970
56.096
17.207
1.00
20.95


ATOM
1418
CE2
TRP
A
247
−12.219
55.756
15.905
1.00
28.03


ATOM
1419
CE3
TRP
A
247
−10.951
55.222
13.904
1.00
22.49


ATOM
1420
CZ2
TRP
A
247
−13.440
55.583
15.232
1.00
31.67


ATOM
1421
CZ3
TRP
A
247
−12.161
55.057
13.238
1.00
25.52


ATOM
1422
CH2
TRP
A
247
−13.388
55.238
13.900
1.00
24.32


ATOM
1423
N
SER
A
248
−7.952
58.162
17.957
1.00
13.59


ATOM
1424
CA
SER
A
248
−8.365
59.069
19.040
1.00
11.50


ATOM
1425
C
SER
A
248
−8.140
60.519
18.634
1.00
9.87


ATOM
1426
O
SER
A
248
−9.010
61.379
18.812
1.00
6.56


ATOM
1427
CB
SER
A
248
−7.577
58.777
20.327
1.00
8.79


ATOM
1428
OG
SER
A
248
−7.657
57.409
20.710
1.00
10.37


ATOM
1429
N
MET
A
249
−6.971
60.800
18.076
1.00
4.51


ATOM
1430
CA
MET
A
249
−6.695
62.162
17.665
1.00
7.99


ATOM
1431
C
MET
A
249
−7.707
62.597
16.631
1.00
9.96


ATOM
1432
O
MET
A
249
−8.232
63.703
16.705
1.00
20.20


ATOM
1433
CB
MET
A
249
−5.287
62.283
17.093
1.00
10.52


ATOM
1434
CG
MET
A
249
−4.995
63.633
16.470
1.00
18.01


ATOM
1435
SD
MET
A
249
−3.294
63.694
15.882
1.00
25.60


ATOM
1436
CE
MET
A
249
−3.492
62.846
14.283
1.00
23.08


ATOM
1437
N
GLY
A
250
−7.998
61.718
15.670
1.00
13.00


ATOM
1438
CA
GLY
A
250
−8.948
62.057
14.620
1.00
7.94


ATOM
1439
C
GLY
A
250
−10.354
62.303
15.116
1.00
9.43


ATOM
1440
O
GLY
A
250
−11.024
63.247
14.677
1.00
11.01


ATOM
1441
N
LEU
A
251
−10.814
61.435
16.013
1.00
11.75


ATOM
1442
CA
LEU
A
251
−12.149
61.575
16.587
1.00
12.10


ATOM
1443
C
LEU
A
251
−12.203
62.901
17.382
1.00
15.74


ATOM
1444
O
LEU
A
251
−13.172
63.665
17.277
1.00
14.37


ATOM
1445
CB
LEU
A
251
−12.439
60.367
17.488
1.00
10.07


ATOM
1446
CG
LEU
A
251
−13.858
59.808
17.652
1.00
17.78


ATOM
1447
CD1
LEU
A
251
−14.247
59.899
19.104
1.00
7.26


ATOM
1448
CD2
LEU
A
251
−14.868
60.557
16.790
1.00
11.79


ATOM
1449
N
SER
A
252
−11.138
63.192
18.136
1.00
13.46


ATOM
1450
CA
SER
A
252
−11.060
64.422
18.944
1.00
18.14


ATOM
1451
C
SER
A
252
−11.135
65.683
18.097
1.00
17.41


ATOM
1452
O
SER
A
252
−11.825
66.627
18.460
1.00
19.27


ATOM
1453
CB
SER
A
252
−9.768
64.447
19.775
1.00
9.91


ATOM
1454
OG
SER
A
252
−9.750
63.359
20.687
1.00
8.34


ATOM
1455
N
LEU
A
253
−10.424
65.696
16.970
1.00
19.18


ATOM
1456
CA
LEU
A
253
−10.432
66.849
16.062
1.00
18.31


ATOM
1457
C
LEU
A
253
−11.790
67.075
15.405
1.00
19.03


ATOM
1458
O
LEU
A
253
−12.163
68.205
15.120
1.00
22.36


ATOM
1459
CB
LEU
A
253
−9.396
66.668
14.962
1.00
19.05


ATOM
1460
CG
LEU
A
253
−7.947
66.985
15.282
1.00
14.67


ATOM
1461
CD1
LEU
A
253
−7.066
66.438
14.166
1.00
12.71


ATOM
1462
CD2
LEU
A
253
−7.778
68.489
15.433
1.00
18.22


ATOM
1463
N
VAL
A
254
−12.524
65.998
15.138
1.00
25.00


ATOM
1464
CA
VAL
A
254
−13.845
66.131
14.526
1.00
25.23


ATOM
1465
C
VAL
A
254
−14.799
66.694
15.576
1.00
26.73


ATOM
1466
O
VAL
A
254
−15.680
67.496
15.260
1.00
28.21


ATOM
1467
CB
VAL
A
254
−14.395
64.755
14.028
1.00
26.92


ATOM
1468
CG1
VAL
A
254
−15.883
64.887
13.736
1.00
25.06


ATOM
1469
CG2
VAL
A
254
−13.628
64.299
12.783
1.00
22.80


ATOM
1470
N
GLU
A
255
−14.628
66.264
16.226
1.00
27.36


ATOM
1471
CA
GLU
A
255
−15.474
66.757
17.920
1.00
23.68


ATOM
1472
C
GLU
A
255
−15.282
68.264
18.119
1.00
24.91


ATOM
1473
O
GLU
A
255
−16.255
69.027
18.150
1.00
20.96


ATOM
1474
CB
GLU
A
255
−15.155
66.048
19.240
1.00
14.74


ATOM
1475
CG
GLU
A
255
−15.884
66.670
20.408
1.00
15.04


ATOM
1476
CD
GLU
A
255
−15.768
65.868
21.677
1.00
21.02


ATOM
1477
OE1
GLU
A
255
−16.519
66.166
22.627
1.00
22.66


ATOM
1478
OE2
GLU
A
255
−14.937
64.942
21.735
1.00
20.57


ATOM
1479
N
MET
A
256
−14.020
68.683
18.253
1.00
24.35


ATOM
1480
CA
MET
A
256
−13.694
70.088
18.462
1.00
25.34


ATOM
1481
C
MET
A
256
−14.119
70.979
17.297
1.00
28.72


ATOM
1482
O
MET
A
256
−14.443
72.148
17.484
1.00
29.34


ATOM
1483
CB
MET
A
256
−12.192
70.236
18.715
1.00
26.97


ATOM
1484
CG
MET
A
256
−11.716
69.502
19.962
1.00
26.86


ATOM
1485
SD
MET
A
256
−10.012
69.864
20.407
1.00
28.01


ATOM
1486
CE
MET
A
256
−9.107
68.604
19.489
1.00
25.72


ATOM
1487
N
ALA
A
257
−14.118
70.417
16.093
1.00
33.65


ATOM
1488
CA
ALA
A
257
−14.508
71.157
14.897
1.00
32.34


ATOM
1489
C
ALA
A
257
−16.031
71.324
14.785
1.00
32.79


ATOM
1490
O
ALA
A
257
−16.500
72.336
14.270
1.00
35.14


ATOM
1491
CB
ALA
A
257
−13.554
70.457
13.653
1.00
31.98


ATOM
1492
N
VAL
A
258
−16.801
70.344
15.265
1.00
30.48


ATOM
1493
CA
VAL
A
258
−18.259
70.432
15.193
1.00
31.53


ATOM
1494
C
VAL
A
258
−18.908
70.857
16.511
1.00
−34.51


ATOM
1495
O
VAL
A
258
−20.099
71.164
16.562
1.00
36.30


ATOM
1496
CB
VAL
A
258
−18.878
69.102
14.734
1.00
29.13


ATOM
1497
CG1
VAL
A
258
−18.213
68.647
13.449
1.00
26.45


ATOM
1498
CG2
VAL
A
258
−18.728
68.055
15.814
1.00
31.99


ATOM
1499
N
GLY
A
259
−18.118
70.885
17.577
1.00
35.42


ATOM
1500
CA
GLY
A
259
−18.643
71.292
18.865
1.00
32.33


ATOM
1501
C
GLY
A
259
−19.520
70.263
19.539
1.00
30.18


ATOM
1502
O
GLY
A
259
−20.454
70.617
20.241
1.00
32.70


ATOM
1503
N
ARG
A
260
−19.222
68.987
19.340
1.00
33.31


ATOM
1504
CA
ARG
A
260
−20.018
67.936
19.956
1.00
33.81


ATOM
1505
C
ARG
A
260
−19.453
66.560
19.603
1.00
32.35


ATOM
1506
O
ARG
A
260
−19.051
66.336
18.465
1.00
32.71


ATOM
1507
CB
ARG
A
260
−21.462
68.075
19.475
1.00
41.22


ATOM
1508
CG
ARG
A
260
−22.343
66.871
19.673
1.00
44.46


ATOM
1509
CD
ARG
A
260
−23.362
66.770
18.542
1.00
46.16


ATOM
1510
NE
ARG
A
260
−23.067
65.631
17.677
1.00
54.94


ATOM
1511
CZ
ARG
A
260
−23.930
65.080
16.830
1.00
54.19


ATOM
1512
NH1
ARG
A
260
−25.165
65.555
16.716
1.00
55.11


ATOM
1513
NH2
ARG
A
260
−23.554
64.043
16.096
1.00
55.19


ATOM
1514
N
TYR
A
261
−19.393
65.662
20.581
1.00
29.73


ATOM
1515
CA
TYR
A
261
−18.890
64.311
20.340
1.00
26.56


ATOM
1516
C
TYR
A
261
−19.621
63.857
19.077
1.00
28.46


ATOM
1517
O
TYR
A
261
−20.844
63.779
19.051
1.00
26.56


ATOM
1518
CB
TYR
A
261
−19.223
63.417
21.525
1.00
20.44


ATOM
1519
CG
TYR
A
261
−18.714
62.010
21.393
1.00
16.63


ATOM
1520
CD1
TYR
A
261
−17.358
61.725
21.466
1.00
12.74


ATOM
1521
CD2
TYR
A
261
−19.600
60.952
21.209
1.00
15.49


ATOM
1522
CE1
TYR
A
261
−16.892
60.414
21.360
1.00
13.47


ATOM
1523
CE2
TYR
A
261
−19.153
59.648
21.101
1.00
12.90


ATOM
1524
CZ
TYR
A
261
−17.799
59.381
21.177
1.00
15.15


ATOM
1525
OH
TYR
A
261
−17.375
58.076
21.075
1.00
9.75


ATOM
1526
N
PRO
A
262
−18.869
63.533
18.022
1.00
29.32


ATOM
1527
CA
PRO
A
262
−19.347
63.105
16.704
1.00
32.21


ATOM
1528
C
PRO
A
262
−19.980
61.726
16.455
1.00
34.38


ATOM
1529
O
PRO
A
262
−20.149
61.331
15.300
1.00
34.69


ATOM
1530
CB
PRO
A
262
−18.124
63.321
15.824
1.00
29.71


ATOM
1531
CG
PRO
A
262
−17.014
62.963
16.716
1.00
30.68


ATOM
1532
CD
PRO
A
262
−17.400
63.500
18.082
1.00
29.38


ATOM
1533
N
ILE
A
263
−20.083
61.326
18.194
1.00
33.38


ATOM
1534
CA
ILE
A
263
−20.946
59.683
17.309
1.00
32.69


ATOM
1535
C
ILE
A
263
−22.204
59.630
18.157
1.00
33.42


ATOM
1536
O
ILE
A
263
−22.145
59.797
19.372
1.00
34.18


ATOM
1537
CB
ILE
A
263
−19.998
58.529
17.700
1.00
31.58


ATOM
1538
CC1
ILE
A
263
−18.636
58.456
16.713
1.00
31.35


ATOM
1539
CG2
ILE
A
263
−20.735
57.213
17.646
1.00
30.37


ATOM
1540
CD1
ILE
A
263
−17.916
57.406
17.055
1.00
32.09


ATOM
1541
N
PRO
A
264
−23.365
59.390
17.531
1.00
35.35


ATOM
1542
CA
PRO
A
264
−23.590
59.162
16.100
1.00
36.67


ATOM
1543
C
PRO
A
264
−23.430
60.426
15.284
1.00
35.40


ATOM
1544
O
PRO
A
264
−23.621
61.526
15.794
1.00
35.56


ATOM
1545
CB
PRO
A
264
−25.021
58.659
16.052
1.00
35.46


ATOM
1546
CG
PRO
A
264
−25.666
59.391
17.171
1.00
36.75


ATOM
1547
CD
PRO
A
264
−24.639
59.405
18.270
1.00
34.29


ATOM
1548
N
PRO
A
265
−23.097
60.284
13.995
1.00
36.51


ATOM
1549
CA
PRO
A
265
−22.916
61.431
13.104
1.00
37.50


ATOM
1550
C
PRO
A
265
−24.013
62.469
13.283
1.00
39.18


ATOM
1551
O
PRO
A
265
−25.160
62.134
13.577
1.00
32.26


ATOM
1552
CB
PRO
A
265
−22.930
60.914
11.708
1.00
36.47


ATOM
1553
CG
PRO
A
265
−23.331
59.370
11.905
1.00
38.04


ATOM
1554
CD
PRO
A
265
−22.887
59.023
13.279
1.00
37.36


ATOM
1555
N
PRO
A
266
−23.665
63.750
13.127
1.00
44.06


ATOM
1556
CA
PRO
A
266
−24.672
64.800
13.284
1.00
48.47


ATOM
1557
C
PRO
A
266
−25.816
64.562
12.314
1.00
51.74


ATOM
1558
O
PRO
A
266
−25.516
64.188
11.156
1.00
51.24


ATOM
1559
CB
PRO
A
266
−23.907
66.086
12.974
1.00
50.13


ATOM
1560
CG
PRO
A
266
−22.459
65.734
13.196
1.00
51.79


ATOM
1561
CD
PRO
A
266
−22.336
64.295
12.802
1.00
47.28


ATOM
1562
N
ASP
A
267
−27.045
64.374
12.771
1.00
52.60


ATOM
1563
N
PRO
A
307
−28.979
60.710
23.903
1.00
65.09


ATOM
1564
CA
PRO
A
307
−29.002
59.318
24.425
1.00
64.51


ATOM
1565
C
PRO
A
307
−27.775
58.466
24.050
1.00
61.30


ATOM
1566
O
PRO
A
307
−26.668
58.983
23.893
1.00
62.13


ATOM
1567
CB
PRO
A
307
−30.290
58.661
23.938
1.00
63.24


ATOM
1568
CG
PRO
A
307
−31.188
59.869
23.597
1.00
64.01


ATOM
1569
CD
PRO
A
307
−30.330
61.154
23.504
1.00
65.27


ATOM
1570
N
MET
A
308
−27.993
57.158
23.925
1.00
57.23


ATOM
1571
CA
MET
A
308
−26.958
56.176
23.588
1.00
48.66


ATOM
1572
C
MET
A
308
−26.084
55.767
24.778
1.00
43.01


ATOM
1573
O
MET
A
308
−25.212
56.516
25.227
1.00
45.77


ATOM
1574
CB
MET
A
308
−26.075
56.675
22.449
1.00
49.51


ATOM
1575
CG
MET
A
308
−25.288
55.561
21.784
1.00
55.77


ATOM
1576
SD
MET
A
308
−25.344
55.652
19.986
1.00
62.75


ATOM
1577
CE
MET
A
308
−26.483
54.349
19.570
1.00
53.22


ATOM
1578
N
ALA
A
309
−26.338
54.563
25.285
1.00
32.29


ATOM
1579
CA
ALA
A
309
−25.595
54.027
26.408
1.00
19.70


ATOM
1580
C
ALA
A
309
−24.164
53.771
25.990
1.00
18.92


ATOM
1581
O
ALA
A
309
−23.823
53.860
24.815
1.00
21.47


ATOM
1582
CB
ALA
A
309
−26.229
52.736
26.877
1.00
19.24


ATOM
1583
N
ILE
A
310
−23.320
53.431
26.950
1.00
21.32


ATOM
1584
CA
ILE
A
310
−21.926
53.179
26.645
1.00
20.61


ATOM
1585
C
ILE
A
310
−21.780
52.016
25.668
1.00
24.69


ATOM
1586
O
ILE
A
310
−21.140
52.150
24.622
1.00
23.49


ATOM
1587
CB
ILE
A
310
−21.145
52.910
27.932
1.00
18.38


ATOM
1588
CG1
ILE
A
310
−21.160
54.179
28.802
1.00
25.45


ATOM
1589
CG2
ILE
A
310
−19.731
52.513
27.601
1.00
16.27


ATOM
1590
CD1
ILE
A
310
−20.720
53.985
30.246
1.00
22.44


ATOM
1591
N
PHE
A
311
−22.369
50.672
26.000
1.00
27.31


ATOM
1592
CA
PHE
A
311
−22.291
49.734
25.097
1.00
25.27


ATOM
1593
C
PHE
A
311
−23.030
50.090
23.801
1.00
23.26


ATOM
1594
O
PHE
A
311
−22.543
49.838
22.699
1.00
19.03


ATOM
1595
CB
PHE
A
311
−22.914
48.436
25.727
1.00
29.96


ATOM
1596
CG
PHE
A
311
−22.876
47.289
24.824
1.00
30.78


ATOM
1597
CD1
PHE
A
311
−21.795
46.426
24.852
1.00
30.28


ATOM
1598
CD2
PHE
A
311
−23.885
47.071
23.896
1.00
29.13


ATOM
1599
CE1
PHE
A
311
−21.715
45.372
23.966
1.00
32.78


ATOM
1600
CE2
PHE
A
311
−23.811
46.020
23.007
1.00
32.18


ATOM
1601
CZ
PHE
A
311
−22.722
45.166
23.041
1.00
31.76


ATOM
1602
N
GLU
A
312
−24.209
50.688
23.936
1.00
17.24


ATOM
1603
CA
GLU
A
312
−24.982
51.083
22.770
1.00
23.14


ATOM
1604
C
GLU
A
312
−24.147
51.872
21.752
1.00
26.51


ATOM
1605
O
GLU
A
312
−24.271
51.674
20.550
1.00
27.72


ATOM
1606
CB
GLU
A
312
−26.183
51.916
23.211
1.00
22.31


ATOM
1607
CG
GLU
A
312
−27.056
52.359
22.061
1.00
32.19


ATOM
1608
CD
GLU
A
312
−28.357
53.013
22.513
1.00
43.74


ATOM
1609
OE1
GLU
A
312
−29.385
52.838
21.816
1.00
47.50


ATOM
1610
OE2
GLU
A
312
−28.360
53.703
23.560
1.00
45.51


ATOM
1611
N
LEU
A
313
−23.290
52.768
22.234
1.00
29.43


ATOM
1612
CA
LEU
A
313
−22.457
53.587
21.354
1.00
23.91


ATOM
1613
C
LEU
A
313
−21.292
52.806
20.731
1.00
24.29


ATOM
1614
O
LEU
A
313
−20.995
52.943
19.535
1.00
19.89


ATOM
1615
CB
LEU
A
313
−21.908
54.790
22.147
1.00
24.50


ATOM
1616
CG
LEU
A
313
−21.357
56.046
21.454
1.00
19.51


ATOM
1617
CD1
LEU
A
313
−19.882
55.874
21.203
1.00
21.95


ATOM
1618
CD2
LEU
A
313
−22.063
56.285
20.143
1.00
26.43


ATOM
1619
N
LEU
A
314
−20.636
51.985
21.546
1.00
21.51


ATOM
1620
CA
LEU
A
314
−19.477
51.223
21.099
1.00
23.89


ATOM
1621
C
LEU
A
314
−19.795
50.107
20.105
1.00
29.16


ATOM
1622
O
LEU
A
314
−18.985
49.800
19.219
1.00
23.78


ATOM
1523
CB
LEU
A
314
−18.739
50.668
22.312
1.00
20.26


ATOM
1624
CG
LEU
A
314
−17.556
51.526
22.787
1.00
27.81


ATOM
1625
CD1
LEU
A
314
−17.917
52.999
22.741
1.00
20.24


ATOM
1626
CD2
LEU
A
314
−17.152
51.113
24.188
1.00
18.09


ATOM
1627
N
ASP
A
315
−21.074
49.773
19.793
1.00
33.42


ATOM
1628
CA
ASP
A
315
−21.378
48.979
18.610
1.00
33.48


ATOM
1629
C
ASP
A
315
−21.336
49.896
17.400
1.00
29.94


ATOM
1630
O
ASP
A
315
−20.965
49.476
16.308
1.00
31.00


ATOM
1631
CB
ASP
A
315
−22.759
48.334
18.738
1.00
38.85


ATOM
1632
CG
ASP
A
315
−23.112
47.471
17.538
1.00
46.48


ATOM
1633
OD1
ASP
A
315
−22.283
46.624
17.123
1.00
46.46


ATOM
1634
OD2
ASP
A
315
−24.230
47.646
17.008
1.00
52.20


ATOM
1635
N
TYR
A
316
−21.692
51.155
17.612
1.00
24.48


ATOM
1636
CA
TYR
A
316
−21.676
52.124
16.537
1.00
25.94


ATOM
1637
C
TYR
A
316
−20.267
52.507
16.082
1.00
28.29


ATOM
1638
O
TYR
A
316
−20.030
52.736
14.896
1.00
30.62


ATOM
1639
CB
TYR
A
316
−22.416
53.395
16.949
1.00
27.97


ATOM
1640
CG
TYR
A
316
−22.757
54.258
15.762
1.00
37.03


ATOM
1641
CD1
TYR
A
316
−21.758
54.936
15.049
1.00
38.41


ATOM
1642
CD2
TYR
A
316
−24.071
54.347
15.306
1.00
40.18


ATOM
1643
CE1
TYR
A
316
−22.064
55.677
13.903
1.00
39.43


ATOM
1644
CE2
TYR
A
316
−24.388
55.083
14.166
1.00
43.05


ATOM
1645
CZ
TYR
A
316
−23.384
55.743
13.468
1.00
44.43


ATOM
1646
OH
TYR
A
316
−23.709
56.440
12.328
1.00
48.33


ATOM
1647
N
ILE
A
317
−19.316
52.594
16.999
1.00
25.68


ATOM
1648
CA
ILE
A
317
−17.993
52.980
16.554
1.00
19.28


ATOM
1649
C
ILE
A
317
−17.296
51.803
15.879
1.00
21.49


ATOM
1650
O
ILE
A
317
−16.550
51.994
14.521
1.00
22.54


ATOM
1651
CB
ILE
A
317
−17.114
53.577
17.724
1.00
18.71


ATOM
1652
CG1
ILE
A
317
−16.120
52.542
18.223
1.00
9.61


ATOM
1653
CG2
ILE
A
317
−17.986
54.046
18.889
1.00
23.94


ATOM
1654
CD1
ILE
A
317
−14.762
52.765
17.699
1.00
9.51


ATOM
1655
N
VAL
A
318
−17.542
50.584
16.347
1.00
22.76


ATOM
1656
CA
VAL
A
318
−16.875
49.447
15.730
1.00
26.45


ATOM
1657
C
VAL
A
318
−17.597
48.889
14.507
1.00
31.54


ATOM
1658
O
VAL
A
318
−16.945
48.465
13.559
1.00
30.25


ATOM
1659
CB
VAL
A
318
−15.633
48.266
16.727
1.00
25.44


ATOM
1660
CG1
VAL
A
318
−16.512
48.775
18.144
1.00
27.71


ATOM
1661
CG2
VAL
A
318
−17.738
47.244
16.614
1.00
25.81


ATOM
1662
N
ASN
A
319
−18.930
48.901
14.525
1.00
33.02


ATOM
1663
CA
ASN
A
319
−19.723
48.354
13.417
1.00
33.39


ATOM
1664
C
ASN
A
319
−20.506
49.356
12.569
1.00
37.02


ATOM
1665
O
ASN
A
319
−21.558
49.022
12.022
1.00
40.88


ATOM
1666
CB
ASN
A
319
−20.696
47.303
13.942
1.00
25.22


ATOM
1667
CG
ASN
A
319
−19.996
46.052
14.370
1.00
30.51


ATOM
1668
OD1
ASN
A
319
−20.403
45.387
15.326
1.00
31.40


ATOM
1669
ND2
ASN
A
319
−18.923
45.717
13.670
1.00
31.28


ATOM
1670
N
GLU
A
320
−20.009
50.579
12.465
1.00
36.63


ATOM
1671
CA
GLU
A
320
−20.664
51.585
11.644
1.00
33.11


ATOM
1672
C
GLU
A
320
−19.545
52.374
11.005
1.00
35.79


ATOM
1673
O
GLU
A
320
−18.377
52.101
11.246
1.00
34.22


ATOM
1674
CB
GLU
A
320
−21.544
52.498
12.486
1.00
25.71


ATOM
1675
CG
GLU
A
320
−22.798
51.842
13.005
1.00
35.24


ATOM
1676
CD
GLU
A
320
−23.810
51.554
11.916
1.00
41.36


ATOM
1677
OE1
GLU
A
320
−23.649
52.084
10.796
1.00
40.25


ATOM
1678
OE2
GLU
A
320
−24.767
50.797
12.190
1.00
42.46


ATOM
1679
N
PRO
A
321
−19.875
53.452
10.128
1.00
40.79


ATOM
1680
CA
PRO
A
321
−18.807
54.136
9.554
1.00
41.65


ATOM
1681
C
PRO
A
321
−18.240
55.205
10.466
1.00
40.06


ATOM
1682
O
PRO
A
321
−18.961
55.805
11.255
1.00
43.82


ATOM
1683
CB
PRO
A
321
−19.482
54.738
8.329
1.00
42.29


ATOM
1684
CG
PRO
A
321
−20.906
54.944
8.772
1.00
44.16


ATOM
1685
CD
PRO
A
321
−21.216
53.851
9.790
1.00
45.10


ATOM
1686
N
PRO
A
322
−16.934
55.454
10.366
1.00
36.15


ATOM
1687
CA
PRO
A
322
−16.320
56.474
11.211
1.00
36.97


ATOM
1688
C
PRO
A
322
−16.904
57.832
10.855
1.00
35.95


ATOM
1689
O
PRO
A
322
−17.417
58.009
9.760
1.00
34.07


ATOM
1690
CB
PRO
A
322
−14.840
56.384
10.853
1.00
36.52


ATOM
1691
CG
PRO
A
322
−14.835
55.823
9.476
1.00
36.70


ATOM
1692
CD
PRO
A
322
−15.953
54.826
9.471
1.00
35.69


ATOM
1693
N
PRO
A
323
−16.868
58.796
11.789
1.00
34.57


ATOM
1694
CA
PRO
A
323
−17.403
60.135
11.510
1.00
34.83


ATOM
1695
C
PRO
A
323
−16.607
60.730
10.346
1.00
36.97


ATOM
1696
O
PRO
A
323
−15.586
60.161
9.949
1.00
37.11


ATOM
1697
CB
PRO
A
323
−17.189
60.889
12.820
1.00
33.19


ATOM
1698
CG
PRO
A
323
−17.066
59.817
13.848
1.00
35.15


ATOM
1699
CD
PRO
A
323
−16.362
58.688
13.162
1.00
34.44


ATOM
1700
N
LYS
A
324
−17.034
61.873
9.813
1.00
38.65


ATOM
1701
CA
LYS
A
324
−16.332
62.410
8.653
1.00
44.36


ATOM
1702
C
LYS
A
324
−16.006
63.890
8.574
1.00
45.09


ATOM
1703
O
LYS
A
324
−15.005
64.257
7.946
1.00
49.78


ATOM
1704
CB
LYS
A
324
−17.096
52.020
7.376
1.00
46.69


ATOM
1705
CG
LYS
A
324
−16.714
60.658
6.791
1.00
53.88


ATOM
1706
CD
LYS
A
324
−16.842
60.633
5.264
1.00
58.03


ATOM
1707
CE
LYS
A
324
−18.219
60.141
4.809
1.00
60.47


ATOM
1708
NZ
LYS
A
324
−19.349
60.935
5.380
1.00
54.66


ATOM
1709
N
LEU
A
325
−16.732
64.824
9.304
1.00
43.22


ATOM
1710
CA
LEU
A
325
−16.537
66.283
9.272
1.00
45.81


ATOM
1711
C
LEU
A
325
−17.379
66.843
8.117
1.00
49.22


ATOM
1712
O
LEU
A
325
−17.138
66.511
6.952
1.00
52.12


ATOM
1713
CB
LEU
A
325
−15.056
66.638
9.047
1.00
39.14


ATOM
1714
CG
LEU
A
325
−14.455
67.922
9.615
1.00
38.72


ATOM
1715
CD1
LEU
A
325
−14.707
67.977
11.109
1.00
37.31


ATOM
1716
CD2
LEU
A
325
−12.953
67.962
9.327
1.00
31.46


ATOM
1717
N
PRO
A
326
−18.360
67.693
8.418
1.00
50.07


ATOM
1718
CA
PRO
A
326
−19.221
68.265
7.359
1.00
51.46


ATOM
1719
C
PRO
A
326
−18.390
66.796
6.199
1.00
52.63


ATOM
1720
O
PRO
A
326
−17.216
69.112
6.367
1.00
54.24


ATOM
1721
CB
PRO
A
326
−19.990
69.387
8.064
1.00
50.91


ATOM
1722
CG
PRO
A
326
−19.333
69.549
9.404
1.00
50.63


ATOM
1723
CD
PRO
A
326
−18.774
68.201
9.741
1.00
50.81


ATOM
3724
N
SER
A
327
−18.992
68.890
5.020
1.00
54.72


ATOM
1725
CA
SER
A
327
−18.259
69.404
3.874
1.00
54.52


ATOM
1726
C
SER
A
327
−18.636
70.844
3.566
1.00
53.41


ATOM
1727
O
SER
A
327
−19.668
71.353
4.022
1.00
49.00


ATOM
1728
CB
SER
A
327
−18.498
68.539
2.634
1.00
55.05


ATOM
1729
OG
SER
A
327
−17.642
68.950
1.578
1.00
53.99


ATOM
1730
N
GLY
A
328
−17.783
71.499
2.789
1.00
53.66


ATOM
1731
CA
GLY
A
328
−18.033
72.877
2.421
1.00
56.94


ATOM
1732
C
GLY
A
328
−17.764
73.838
3.558
1.00
57.41


ATOM
1733
O
GLY
A
328
−17.424
75.000
3.329
1.00
59.46


ATOM
1734
N
VAL
A
329
−17.925
73.354
4.787
1.00
56.20


ATOM
1735
CA
VAL
A
329
−17.682
74.171
5.969
1.00
52.30


ATOM
1736
C
VAL
A
329
−16.195
74.073
6.339
1.00
51.10


ATOM
1737
O
VAL
A
329
−15.653
74.955
7.012
1.00
50.96


ATOM
1738
CB
VAL
A
329
−18.545
73.696
7.171
1.00
52.02


ATOM
1739
CG1
VAL
A
329
−18.566
74.769
8.244
1.00
49.49


ATOM
1740
CG2
VAL
A
329
−19.964
73.369
6.711
1.00
49.32


ATOM
1741
N
PHE
A
330
−15.549
73.001
5.882
1.00
47.04


ATOM
1742
CA
PHE
A
330
−14.132
72.759
6.152
1.00
44.27


ATOM
1743
C
PHE
A
330
−13.355
72.401
4.892
1.00
44.37


ATOM
1744
O
PHE
A
330
−13.841
71.660
4.032
1.00
42.88


ATOM
1745
CB
PHE
A
330
−13.959
71.618
7.161
1.00
39.38


ATOM
1746
CG
PHE
A
330
−14.573
71.890
8.491
1.00
34.06


ATOM
1747
CD1
PHE
A
330
−13.901
72.652
9.435
1.00
26.26


ATOM
2748
CD2
PHE
A
330
−15.839
71.395
8.794
1.00
31.05


ATOM
1749
CE1
PHE
A
330
−14.485
72.917
10.671
1.00
29.71


ATOM
1750
CE2
PHE
A
330
−16.431
71.654
10.031
1.00
29.80


ATOM
1751
CZ
PHE
A
330
−15.756
72.416
10.972
1.00
24.30


ATOM
1752
N
SER
A
331
−12.131
72.914
4.812
1.00
44.31


ATOM
1753
CA
SER
A
331
−11.250
72.673
3.682
1.00
42.02


ATOM
1754
C
SER
A
331
−11.127
71.190
3.353
1.00
42.62


ATOM
1755
O
SER
A
331
−11.247
70.335
4.225
1.00
43.55


ATOM
1756
CB
SER
A
331
−9.865
73.240
3.972
1.00
40.13


ATOM
1757
OG
SER
A
331
−8.911
72.198
4.028
1.00
42.50


ATOM
1758
N
LEU
A
332
−10.887
70.903
2.080
1.00
43.03


ATOM
1759
CA
LEU
A
332
−10.740
69.538
1.608
1.00
43.70


ATOM
1760
C
LEU
A
332
−9.545
68.899
2.296
1.00
44.35


ATOM
1761
O
LEU
A
332
−9.576
67.710
2.616
1.00
45.21


ATOM
1762
CB
LEU
A
332
−10.528
69.524
0.089
1.00
44.08


ATOM
1763
CG
LEU
A
332
−11.712
69.393
−0.882
1.00
44.77


ATOM
1764
CD1
LEU
A
332
−11.629
68.029
−1.542
1.00
43.67


ATOM
1765
CD2
LEU
A
332
−13.055
69.574
−0.180
1.00
42.40


ATOM
1766
N
GLU
A
333
−8.495
69.693
2.515
1.00
43.47


ATOM
1767
CA
GLU
A
333
−7.273
69.217
3.168
1.00
44.27


ATOM
1768
C
GLU
A
333
−7.568
68.638
4.551
1.00
44.90


ATOM
1769
O
GLU
A
333
−7.181
67.507
4.860
1.00
42.45


ATOM
1770
CB
GLU
A
333
−6.278
70.362
3.321
1.00
46.83


ATOM
1771
CG
GLU
A
333
−5.034
70.216
2.471
1.00
56.47


ATOM
1772
CD
GLU
A
333
−4.811
77.418
1.565
1.00
61.64


ATOM
1773
OE1
GLU
A
333
−3.665
71.606
1.087
1.00
63.78


ATOM
1774
OE2
GLU
A
333
−5.787
72.170
1.334
1.00
61.66


ATOM
1775
N
PHE
A
334
−8.235
69.434
5.381
1.00
43.71


ATOM
1776
CA
PHE
A
334
−8.603
69.027
5.730
1.00
42.62


ATOM
1777
C
PHE
A
334
−9.446
67.756
6.654
1.00
44.19


ATOM
1778
O
PHE
A
334
−9.180
66.782
7.350
1.00
49.41


ATOM
1779
CB
PHE
A
334
−9.394
70.153
7.406
1.00
41.89


ATOM
1780
CG
PHE
A
334
−9.711
69.910
8.859
1.00
39.29


ATOM
1781
CD1
PHE
A
334
−8.980
69.003
9.614
1.00
39.69


ATOM
1782
CD2
PHE
A
334
−10.742
70.615
9.475
1.00
38.19


ATOM
1783
CE1
PHE
A
334
−9.273
68.806
10.953
1.00
39.69


ATOM
1784
CE2
PHE
A
334
−11.040
70.424
10.811
1.00
35.73


ATOM
1785
CZ
PHE
A
334
−10.306
69.518
11.554
1.00
39.02


ATOM
1786
N
GLN
A
335
−10.456
67.758
5.792
1.00
40.70


ATOM
1787
CA
GLN
A
335
−11.311
66.592
5.661
1.00
38.96


ATOM
1788
C
GLN
A
335
−10.501
65.314
5.410
1.00
38.54


ATOM
1789
O
GLN
A
335
−10.724
64.295
6.073
1.00
36.94


ATOM
1790
CB
GLN
A
335
−12.334
66.829
4.545
1.00
40.63


ATOM
1791
CG
GLN
A
335
−13.257
68.023
4.813
1.00
40.03


ATOM
1792
CD
GLN
A
335
−14.396
68.137
3.808
1.00
40.97


ATOM
1793
OE1
GLN
A
335
−14.730
69.233
3.345
1.00
40.86


ATOM
1794
NE2
GLN
A
335
−14.996
67.005
3.469
1.00
36.03


ATOM
1795
N
ASP
A
336
−9.556
65.371
4.473
1.00
38.02


ATOM
1796
CA
ASP
A
336
−8.715
64.211
4.155
1.00
38.81


ATOM
1797
C
ASP
A
336
−7.931
63.778
5.382
1.00
37.31


ATOM
1798
O
ASP
A
336
−7.910
62.597
5.733
1.00
41.15


ATOM
1799
CB
ASP
A
336
−7.725
64.537
3.021
1.00
43.06


ATOM
1800
CG
ASP
A
336
−6.986
63.299
2.501
1.00
43.28


ATOM
1801
OD1
ASP
A
336
−7.654
62.374
1.989
1.00
39.54


ATOM
1802
OD2
ASP
A
336
−5.739
63.246
2.603
1.00
42.70


ATOM
1803
N
PHE
A
337
−7.280
64.743
6.028
1.00
33.36


ATOM
1804
CA
PHE
A
337
−6.491
64.474
7.227
1.00
31.84


ATOM
1805
C
PHE
A
337
−7.304
63.670
8.252
1.00
28.10


ATOM
1806
O
PHE
A
337
−6.901
62.582
8.657
1.00
25.73


ATOM
1807
CB
PHE
A
337
−6.014
65.792
7.843
1.00
28.41


ATOM
1808
CG
PHE
A
337
−5.097
65.616
9.011
1.00
32.15


ATOM
1809
CD1
PHE
A
337
−5.575
65.753
10.317
1.00
31.68


ATOM
1810
CD2
PHE
A
337
−3.760
65.300
8.816
1.00
30.96


ATOM
1811
CE1
PHE
A
337
−4.736
65.576
11.408
1.00
32.28


ATOM
1812
CE2
PHE
A
337
−2.907
65.119
9.905
1.00
32.34


ATOM
1813
CZ
PHE
A
337
−3.398
65.258
11.205
1.00
34.20


ATOM
1814
N
VAL
A
338
−8.450
64.214
8.652
1.00
26.17


ATOM
1815
CA
VAL
A
338
−9.327
63.568
9.616
1.00
24.52


ATOM
1816
C
VAL
A
338
−9.675
62.186
9.107
1.00
27.76


ATOM
1817
O
VAL
A
338
−9.601
61.195
9.841
1.00
30.23


ATOM
1818
CB
VAL
A
338
−10.633
64.353
9.777
1.00
23.80


ATOM
1819
CG1
VAL
A
338
−11.742
63.430
10.234
1.00
30.94


ATOM
1820
CG2
VAL
A
338
−10.438
65.479
10.759
1.00
25.08


ATOM
1821
N
ASN
A
339
−10.052
62.126
7.836
1.00
29.15


ATOM
1822
CA
ASN
A
339
−10.434
60.870
7.227
1.00
28.27


ATOM
1823
C
ASN
A
339
−9.328
59.815
7.236
1.00
26.42


ATOM
1824
O
ASN
A
339
−9.612
68.617
7.361
1.00
27.22


ATOM
1825
CB
ASN
A
339
−10.938
61.126
5.809
1.00
35.10


ATOM
1826
CG
ASN
A
339
−12.421
61.453
5.776
1.00
41.02


ATOM
1827
OD1
ASN
A
339
−12.836
62.567
6.120
1.00
46.01


ATOM
1828
ND2
ASN
A
339
−13.234
60.476
5.375
1.00
44.68


ATOM
1829
N
LYS
A
340
−8.139
60.129
7.011
1.00
23.28


ATOM
1830
CA
LYS
A
340
−7.017
59.194
7.022
1.00
23.48


ATOM
1831
C
LYS
A
340
−6.748
58.632
8.422
1.00
23.77


ATOM
1832
O
LYS
A
340
−6.103
57.585
8.573
1.00
21.60


ATOM
1833
CB
LYS
A
240
−5.760
59.388
6.497
1.00
28.68


ATOM
1834
CG
LYS
A
340
−5.921
60.499
5.117
1.00
26.60


ATOM
1835
CD
LYS
A
340
−4.611
60.442
4.333
1.00
37.57


ATOM
1836
CE
LYS
A
340
−4.672
59.429
3.188
1.00
41.31


ATOM
1637
NZ
LYS
A
340
−5.724
59.780
2.190
1.00
39.04


ATOM
1838
N
CYS
A
341
−7.246
59.342
9.432
1.00
21.69


ATOM
1839
CA
CYS
A
341
−7.090
58.952
10.631
1.00
25.76


ATOM
1840
C
CYS
A
341
−8.236
58.049
11.233
1.00
26.90


ATOM
1841
O
CYS
A
341
−8.067
57.146
12.049
1.00
25.45


ATOM
1842
CB
CYS
A
341
−7.143
60.178
11.756
1.00
22.44


ATOM
1843
SG
CYS
A
341
−5.858
61.391
11.554
1.00
21.34


ATOM
1844
N
LEU
A
342
−9.412
58.314
10.664
1.00
26.83


ATOM
1845
CA
LEU
A
342
−10.609
57.559
11.008
1.00
22.24


ATOM
1846
C
LEU
A
342
−10.884
56.323
10.164
1.00
26.89


ATOM
1847
O
LEU
A
342
−12.032
55.885
10.038
1.00
27.72


ATOM
1848
CB
LEU
A
342
−11.809
58.511
11.029
1.00
17.16


ATOM
1849
CG
LEU
A
342
−11.636
59.620
12.096
1.00
18.71


ATOM
1850
CD1
LEU
A
342
−12.796
60.613
12.071
1.00
15.80


ATOM
1851
CD2
LEU
A
342
−11.540
58.967
13.475
1.00
7.33


ATOM
1852
N
ILE
A
343
−9.819
55.753
9.599
1.00
26.64


ATOM
1853
CA
ILE
A
343
−9.912
54.538
8.794
1.00
24.35


ATOM
1854
C
ILE
A
343
−10.004
53.379
9.783
1.00
26.29


ATOM
1855
O
ILE
A
343
−9.062
53.106
10.522
1.00
25.94


ATOM
1856
CB
ILE
A
343
−8.651
54.325
7.920
1.00
26.61


ATOM
1857
CG1
ILE
A
343
−8.690
55.239
6.694
1.00
29.30


ATOM
1858
CG2
ILE
A
343
−8.570
52.882
7.468
1.00
25.17


ATOM
1859
CD1
ILE
A
343
−7.376
55.296
5.942
1.00
32.35


ATOM
1860
N
LYS
A
344
−11.135
52.691
9.793
1.00
24.72


ATOM
1861
CA
LYS
A
344
−11.324
51.585
10.712
1.00
24.40


ATOM
1862
C
LYS
A
344
−10.166
50.601
10.830
1.00
24.06


ATOM
1863
O
LYS
A
344
−9.872
50.130
11.925
1.00
29.34


ATOM
1864
CB
LYS
A
344
−12.587
50.831
10.348
1.00
21.72


ATOM
1865
CG
LYS
A
344
−13.805
51.310
11.086
1.00
25.93


ATOM
1866
CD
LYS
A
344
−14.477
50.134
11.773
1.00
22.29


ATOM
1867
CE
LYS
A
344
−15.947
50.115
11.433
1.00
27.12


ATOM
1866
NZ
LYS
A
344
−16.436
51.495
11.269
1.00
27.32


ATOM
1869
N
ASN
A
345
−9.504
50.273
9.729
1.00
23.75


ATOM
1870
CA
ASN
A
345
−8.404
49.313
9.805
1.00
20.16


ATOM
1871
C
ASN
A
345
−7.086
49.969
10.206
1.00
19.86


ATOM
1872
O
ASN
A
345
−6.597
50.882
9.527
1.00
22.22


ATOM
1873
CB
ASN
A
345
−8.230
48.585
8.480
1.00
16.87


ATOM
1874
CG
ASN
A
345
−7.263
47.441
8.590
1.00
18.21


ATOM
1875
OD1
ASN
A
345
−7.668
46.295
8.721
1.00
28.21


ATOM
1876
ND2
ASN
A
345
−5.975
47.744
8.560
1.00
21.14


ATOM
1677
N
PRO
A
346
−6.469
49.473
11.293
1.00
16.28


ATOM
1878
CA
PRO
A
346
−5.198
49.979
11.847
1.00
17.23


ATOM
1879
C
PRO
A
346
−4.029
50.055
10.870
1.00
18.68


ATOM
1880
O
PRO
A
346
−3.377
51.099
10.752
1.00
15.58


ATOM
1881
CB
PRO
A
346
−4.897
49.037
13.021
1.00
15.88


ATOM
1882
CG
PRO
A
346
−6.175
48.340
13.320
1.00
15.67


ATOM
1883
CD
PRO
A
346
−6.989
48.318
12.042
1.00
13.71


ATOM
1884
N
ALA
A
347
−3.768
48.947
10.177
1.00
20.95


ATOM
1885
CA
ALA
A
347
−2.670
48.870
9.208
1.00
16.75


ATOM
1886
C
ALA
A
347
−2.936
49.806
8.029
1.00
15.22


ATOM
1887
O
ALA
A
347
−2.031
50.477
7.509
1.00
14.33


ATOM
1888
CB
ALA
A
347
−2.511
47.446
8.739
1.00
14.19


ATOM
1889
N
GLU
A
346
−4.190
49.886
7.631
1.00
15.51


ATOM
1890
CA
GLU
A
348
−4.546
50.766
6.534
1.00
19.61


ATOM
1891
CB
GLU
A
348
−5.959
50.445
6.035
1.00
18.97


ATOM
1892
C
GLU
A
348
−4.458
52.213
7.009
1.00
21.39


ATOM
1893
O
GLU
A
348
−3.875
53.060
6.336
1.00
27.15


ATOM
1894
N
ARG
A
349
−5.039
52.490
8.173
1.00
20.69


ATOM
1895
CA
ARG
A
349
−5.027
53.838
3.746
1.00
17.92


ATOM
1896
C
ARG
A
349
−3.654
54.460
8.637
1.00
7.78


ATOM
1897
O
ARG
A
349
−2.649
53.765
8.765
1.00
12.41


ATOM
1898
CB
ARG
A
349
−5.415
53.773
10.224
1.00
20.98


ATOM
1899
CG
ARG
A
349
−5.710
55.118
10.874
1.30
17.06


ATOM
1900
CD
ARG
A
349
−6.733
54.931
12.000
1.00
14.66


ATOM
1901
NE
ARG
A
349
−6.288
53.989
13.018
1.00
6.25


ATOM
1902
CZ
ARG
A
349
−7.049
53.037
13.535
1.00
12.99


ATOM
1903
NH1
ARG
A
349
−8.293
52.895
13.122
1.00
16.90


ATOM
1904
NH2
ARG
A
349
−6.578
52.245
14.488
1.00
17.23


ATOM
1905
N
ALA
A
350
−3.600
55.762
8.389
1.00
6.21


ATOM
1906
CA
ALA
A
350
−2.309
86.442
8.319
1.00
9.41


ATOM
1907
C
ALA
A
350
−1.609
56.336
9.667
1.00
15.70


ATOM
1908
O
ALA
A
350
−2.242
56.119
13.711
1.00
13.12


ATOM
1909
CB
ALA
A
350
−2.491
57.908
7.968
1.00
6.10


ATOM
1910
N
ASP
A
351
−0.297
56.497
9.639
1.00
15.82


ATOM
1911
CA
ASP
A
351
0.498
56.440
10.842
1.90
21.67


ATOM
1912
C
ASP
A
351
1.177
57.812
11.031
1.00
24.56


ATOM
1913
O
ASP
A
351
1.020
58.706
10.194
1.00
29.51


ATOM
1914
CB
ASP
A
351
1.519
55.303
10.727
1.00
18.58


ATOM
1915
CG
ASP
A
351
2.700
55.668
9.851
1.00
20.97


ATOM
1916
OD1
ASP
A
351
2.579
56.613
9.035
1.00
16.93


ATOM
1917
OD2
ASP
A
351
3.755
55.008
9.986
1.00
23.35


ATOM
1918
N
LEU
A
352
1.922
57.973
12.121
1.00
24.09


ATOM
1919
CA
LEU
A
352
2.590
59.241
12.438
1.00
23.69


ATOM
1920
C
LEU
A
352
3.457
59.795
11.310
1.00
21.24


ATOM
1921
O
LEU
A
352
3.360
60.975
10.973
1.00
23.54


ATOM
1922
CB
LEU
A
352
3.436
59.081
13.718
1.00
17.72


ATOM
1923
CG
LEU
A
352
2.856
59.475
15.084
1.00
14.59


ATOM
1924
CD1
LEU
A
352
1.413
59.786
14.971
1.00
10.57


ATOM
1925
CD2
LEU
A
352
3.071
58.361
16.082
1.00
14.58


ATOM
1926
N
LYS
A
353
4.301
58.948
10.733
1.00
22.47


ATOM
1927
CA
LYS
A
353
5.193
59.336
9.640
1.00
26.48


ATOM
1928
C
LYS
A
353
4.473
60.059
8.511
1.00
27.20


ATOM
1929
O
LYS
A
353
4.901
61.120
8.055
1.90
21.83


ATOM
1930
CB
LYS
A
353
5.863
58.096
9.050
1.00
32.21


ATOM
1931
CG
LYS
A
353
7.319
57.912
9.450
1.00
45.37


ATOM
1932
CD
LYS
A
353
7.549
56.584
10.193
1.00
55.46


ATOM
1933
CE
LYS
A
353
7.614
55.382
9.241
1.00
56.01


ATOM
1934
NZ
LYS
A
353
7.202
54.101
9.911
1.00
57.64


ATOM
1935
N
GLN
A
354
3.378
59.462
8.054
1.00
28.69


ATOM
1936
CA
GLN
A
354
2.609
60.025
6.958
1.00
29.15


ATOM
1937
C
GLN
A
354
1.833
61.270
7.325
1.00
31.90


ATOM
1938
O
GLN
A
354
1.912
62.277
6.623
1.00
34.48


ATOM
1939
CB
GLN
A
354
1.664
58.975
6.398
1.00
26.68


ATOM
1940
CG
GLN
A
354
2.379
57.740
5.872
1.00
29.55


ATOM
1941
CD
GLN
A
354
1.415
56.611
5.586
1.00
28.22


ATOM
1942
OE1
GLN
A
354
0.254
56.676
5.975
1.09
34.18


ATOM
1943
NE2
GLN
A
354
1.885
55.572
4.905
1.00
33.76


ATOM
1944
N
LEU
A
355
1.078
61.211
8.416
1.00
32.07


ATOM
1945
CA
LEU
A
355
0.310
62.381
8.831
1.00
28.51


ATOM
1945
C
LEU
A
355
1.264
63.576
8.928
1.00
29.22


ATOM
1947
O
LEU
A
355
0.875
64.706
2.636
1.00
24.91


ATOM
1948
CB
LEU
A
355
−0.371
62.134
10.186
1.00
27.44


ATOM
1949
CG
LEU
A
355
−1.501
61.101
10.276
1.00
28.08


ATOM
1950
CD1
LEU
A
355
−1.976
61.000
11.721
1.00
24.11


ATOM
1951
CD2
LEU
A
355
−2.657
61.498
9.367
1.00
20.45


ATOM
1952
N
MET
A
356
2.512
63.322
9.322
1.00
31.07


ATOM
1953
CA
MET
A
356
3.500
64.396
9.451
1.00
37.13


ATOM
1954
C
MET
A
356
3.764
65.079
8.118
1.00
38.03


ATOM
1955
O
MET
A
356
4.056
66.273
8.073
1.00
41.67


ATOM
1956
CB
MET
A
356
4.835
63.865
9.993
1.00
39.54


ATOM
1957
CG
MET
A
356
4.945
63.819
11.517
1.00
49.00


ATOM
1958
SD
MET
A
356
5.656
65.295
12.314
1.00
53.92


ATOM
1959
CE
MET
A
356
4.721
66.612
11.503
1.00
47.94


ATOM
1960
N
VAL
A
357
3.680
64.323
7.033
1.00
36.93


ATOM
1961
CA
VAL
A
357
3.929
64.892
5.719
1.00
36.19


ATOM
1962
C
VAL
A
357
2.639
65.162
4.965
1.00
39.27


ATOM
1963
O
VAL
A
357
2.677
65.482
3.779
1.00
40.56


ATOM
1964
CB
VAL
A
357
4.824
63.965
4.867
1.00
36.30


ATOM
1965
CG1
VAL
A
357
6.084
63.616
5.641
1.00
28.89


ATOM
1966
CG2
VAL
A
357
4.060
62.698
4.475
1.00
33.20


ATOM
1967
N
HIS
A
358
1.501
65.042
5.650
1.00
38.28


ATOM
1968
CA
HIS
A
358
0.199
65.273
5.024
1.00
32.30


ATOM
1969
C
HIS
A
358
0.000
66.734
4.675
1.00
36.28


ATOM
1970
O
HIS
A
358
0.495
67.622
5.362
1.00
36.14


ATOM
1971
CB
HIS
A
358
−0.931
64.820
5.946
1.00
26.95


ATOM
1972
CG
HIS
A
358
−2.278
64.773
5.288
1.00
22.17


ATOM
1973
ND1
HIS
A
359
−3.046
65.901
5.080
1.00
19.46


ATOM
1974
CD2
HIS
A
358
−3.013
63.730
4.838
1.00
12.82


ATOM
1975
CE1
HIS
A
358
−4.198
65.552
4.534
1.00
19.53


ATOM
1976
NE2
HIS
A
358
−4.200
64.239
4.377
1.00
20.08


ATOM
1977
N
ALA
A
359
−0.738
66.970
3.599
1.00
39.27


ATOM
1979
CA
ALA
A
359
−0.993
68.324
3.136
1.00
40.52


ATOM
1979
C
ALA
A
359
−1.546
69.225
4.222
1.00
42.82


ATOM
1980
O
ALA
A
359
−1.062
70.342
4.408
1.00
46.44


ATOM
1981
CB
ALA
A
359
−1.951
68.299
1.960
1.00
40.31


ATOM
1982
N
PHE
A
360
−2.560
68.746
4.937
1.00
42.80


ATOM
1983
CA
PHE
A
360
−3.182
69.559
5.976
1.00
41.30


ATOM
1984
C
PHE
A
360
−2.199
70.181
6.957
1.00
36.01


ATOM
1985
O
PHE
A
360
−2.283
71.371
7.255
1.00
36.96


ATOM
1986
CB
PHE
A
360
−4.223
68.750
6.753
1.00
41.54


ATOM
1937
CG
PHE
A
360
−4.868
69.523
7.864
1.00
41.26


ATOM
1988
CD1
PHE
A
360
−5.768
70.551
7.581
1.00
44.60


ATOM
1989
CD2
PHE
A
360
−4.551
69.256
9.195
1.00
39.00


ATOM
1990
CE1
PHE
A
360
−6.344
71.306
8.605
1.00
42.18


ATOM
1991
CE2
PHE
A
360
−5.118
70.002
10.226
1.00
38.72


ATOM
1992
CZ
PHE
A
360
−6.017
71.031
9.930
1.00
40.54


ATOM
1993
N
ILE
A
351
−1.269
69.399
7.472
1.00
34.40


ATOM
1994
CA
ILE
A
361
−0.339
69.979
8.410
1.00
34.72


ATOM
1995
C
ILE
A
361
0.708
70.806
7.686
1.00
36.39


ATOM
1996
O
ILE
A
361
1.086
71.870
8.170
1.00
42.25


ATOM
1997
CB
ILE
A
361
0.319
68.911
9.332
1.00
34.20


ATOM
1998
CG1
ILE
A
361
1.480
68.235
8.627
1.00
32.14


ATOM
1999
CG2
ILE
A
361
−0.722
67.911
9.794
1.00
33.00


ATOM
2000
CD1
ILE
A
361
2.777
68.476
9.341
1.00
33.06


ATOM
2001
N
LYS
A
362
1.165
70.352
6.517
1.00
37.29


ATOM
2002
CA
LYS
A
362
2.161
71.112
5.747
1.00
33.35


ATOM
2003
C
LYS
A
362
1.624
72.514
5.480
1.00
31.71


ATOM
2004
O
LYS
A
362
2.337
73.503
5.634
1.00
29.19


ATOM
2005
CB
LYS
A
362
2.478
70.409
4.425
1.00
34.07


ATOM
2006
CG
LYS
A
362
3.415
69.219
4.573
1.00
36.58


ATOM
2007
CD
LYS
A
362
4.231
68.992
3.311
1.00
43.23


ATOM
2008
CE
LYS
A
362
5.666
68.560
3.638
1.00
48.51


ATOM
2009
NZ
LYS
A
362
6.732
69.524
3.132
1.00
46.38


ATOM
2010
N
ARG
A
363
0.361
72.590
5.075
1.00
22.76


ATOM
2011
CA
ARG
A
363
−0.279
73.873
4.829
1.00
36.19


ATOM
2012
C
ARG
A
363
−0.639
74.473
6.180
1.00
33.31


ATOM
2013
O
ARG
A
363
−0.994
75.645
6.272
1.00
39.69


ATOM
2014
CB
ARG
A
363
−1.562
73.706
3.999
1.00
37.74


ATOM
2015
CG
ARG
A
363
−2.463
74.958
3.984
1.00
40.97


ATOM
2016
CD
ARG
A
363
−3.971
74.638
3.980
1.00
43.17


ATOM
2017
NE
ARG
A
363
−4.581
74.736
5.309
1.00
45.24


ATOM
2018
CZ
ARG
A
363
−5.764
74.216
5.636
1.00
44.99


ATOM
2019
NH1
ARG
A
363
−6.473
73.559
4.728
1.00
45.04


ATOM
2020
NH2
ARG
A
363
−6.232
74.339
6.871
1.00
42.98


ATOM
2021
N
SER
A
364
−0.543
73.664
7.232
1.00
41.94


ATOM
2022
CA
SER
A
364
−0.884
74.125
8.574
1.00
44.68


ATOM
2023
C
SER
A
364
0.274
74.720
9.373
1.00
44.51


ATOM
2024
O
SER
A
364
0.154
75.820
9.905
1.00
44.42


ATOM
2025
CB
SER
A
364
−1.530
72.993
9.370
1.00
42.64


ATOM
2026
OG
SER
A
364
−2.297
73.521
10.428
1.00
42.96


ATOM
2027
N
ASP
A
365
1.393
74.006
9.473
1.00
46.88


ATOM
2028
CA
ASP
A
365
2.525
74.547
10.220
1.00
51.48


ATOM
2029
C
ASP
A
365
3.240
75.596
9.387
1.00
53.14


ATOM
2030
O
ASP
A
365
4.372
75.980
9.678
1.00
53.14


ATOM
2031
CB
ASP
A
365
3.513
73.444
10.638
1.00
51.70


ATOM
2032
CG
ASP
A
365
3.935
72.566
9.490
1.00
50.62


ATOM
2033
OD1
ASP
A
365
3.307
72.658
8.416
1.00
52.17


ATOM
2034
OD2
ASP
A
365
4.893
71.780
9.664
1.00
46.70


ATOM
2035
N
ALA
A
366
2.560
76.051
8.343
1.00
56.72


ATOM
2036
CA
ALA
A
366
3.083
77.074
7.458
1.00
57.10


ATOM
2037
C
ALA
A
366
2.042
78.179
7.412
1.00
59.35


ATOM
2038
O
ALA
A
366
1.864
78.832
6.389
1.00
63.04


ATOM
2039
CB
ALA
A
366
3.308
76.503
6.072
1.00
55.61


ATOM
2040
N
GLU
A
367
1.348
78.378
8.527
1.00
60.82


ATOM
2041
CA
GLU
A
367
0.314
79.399
8.609
1.00
61.72


ATOM
2042
C
GLU
A
367
0.671
80.477
9.627
1.00
62.67


ATOM
2043
O
GLU
A
367
1.685
80.373
10.312
1.00
61.46


ATOM
2044
CB
GLU
A
367
−1.027
78.751
8.961
1.00
64.20


ATOM
2045
CG
GLU
A
367
−1.915
78.474
7.750
1.00
69.00


ATOM
2046
CD
GLU
A
367
−2.928
77.354
7.984
1.00
73.74


ATOM
2047
OE1
GLU
A
367
−3.008
76.826
9.116
1.00
76.77


ATOM
2048
OE2
GLU
A
367
−3.647
77.002
7.024
1.00
75.15


ATOM
2049
N
GLU
A
368
−0.176
81.502
9.722
1.00
9.722


ATOM
2050
CA
GLU
A
368
0.035
82.633
10.626
1.00
67.48


ATOM
2051
C
GLU
A
368
−0.467
82.454
12.067
1.00
69.16


ATOM
2052
O
GLU
A
368
0.331
82.158
12.960
1.00
70.91


ATOM
2053
CB
GLU
A
368
−0.594
83.899
10.020
1.00
71.00


ATOM
2054
CG
GLU
A
368
0.343
84.694
9.093
1.00
75.97


ATOM
2055
CD
GLU
A
368
−0.373
85.335
7.895
1.00
76.77


ATOM
2056
OE1
GLU
A
368
0.215
85.357
6.786
1.00
76.77


ATOM
2057
OE2
GLU
A
368
−1.518
85.816
8.060
1.00
76.77


ATOM
2058
N
VAL
A
369
−1.772
82.638
12.286
1.00
68.33


ATOM
2059
CA
VAL
A
369
−2.422
82.532
13.615
1.00
66.88


ATOM
2060
C
VAL
A
369
−1.519
82.311
14.830
1.00
64.85


ATOM
2061
O
VAL
A
369
−0.774
81.333
14.894
1.00
63.15


ATOM
2062
CB
VAL
A
369
−3.507
81.433
13.638
1.00
66.81


ATOM
2063
CG1
VAL
A
369
−4.656
81.816
12.706
1.00
66.26


ATOM
2064
CG2
VAL
A
369
−2.900
80.089
13.264
1.00
61.40


ATOM
2065
N
ASP
A
370
−1.614
83.213
15.805
1.00
63.73


ATOM
2066
CA
ASP
A
370
−0.783
83.134
17.008
1.00
66.12


ATOM
2067
C
ASP
A
370
−1.274
82.117
18.030
1.00
64.72


ATOM
2068
O
ASP
A
370
−0.530
81.720
18.939
1.00
66.39


ATOM
2069
CB
ASP
A
370
−0.682
84.518
17.674
1.00
66.32


ATOM
2070
CG
ASP
A
370
−1.942
84.901
18.430
1.00
67.73


ATOM
2071
OD1
ASP
A
370
−1.883
85.885
19.202
1.00
65.69


ATOM
2072
OD2
ASP
A
370
−2.985
84.229
13.253
1.00
68.04


ATOM
2073
N
PHE
A
371
−2.520
81.690
17.864
1.00
59.14


ATOM
2074
CA
PHE
A
371
−3.129
80.736
18.778
1.00
53.87


ATOM
2075
C
PHE
A
371
−3.197
81.359
20.157
1.00
50.88


ATOM
2076
O
PHE
A
371
−4.287
31.628
20.669
1.00
48.84


ATOM
2077
CB
PHE
A
371
−2.321
79.443
18.861
1.00
48.42


ATOM
2078
CG
PHE
A
371
−2.924
78.440
19.782
1.00
44.83


ATOM
2079
CD1
PHE
A
371
−2.420
78.266
21.063
1.00
45.11


ATOM
2080
CD2
PHE
A
371
−4.055
77.729
19.401
1.00
43.24


ATOM
2081
CE1
PHE
A
371
−3.041
77.400
21.961
1.00
43.17


ATOM
2082
CE2
PHE
A
371
−4.680
76.863
20.238
1.00
44.90


ATOM
2083
CZ
PHE
A
371
−4.175
76.699
21.572
1.00
42.52


ATOM
2084
N
ALA
A
372
−2.024
81.587
20.746
1.00
47.94


ATOM
2085
CA
ALA
A
372
−1.905
82.192
22.059
1.00
45.39


ATOM
2086
C
ALA
A
372
−2.929
83.307
22.250
1.00
45.44


ATOM
2087
O
ALA
A
372
−3.486
83.484
23.332
1.00
47.00


ATOM
2088
CB
ALA
A
372
−0.505
82.734
22.256
1.00
44.48


ATOM
2089
N
GLY
A
373
−3.176
84.058
21.181
1.00
45.75


ATOM
2390
CA
GLY
A
373
−4.136
85.141
21.249
1.00
44.66


ATOM
2091
C
GLY
A
373
−5.567
84.645
21.228
1.00
46.58


ATOM
2092
O
GLY
A
373
−6.381
85.029
22.074
1.00
46.98


ATOM
2093
N
TRP
A
374
−5.876
83.783
20.261
1.00
46.70


ATOM
2094
CA
TRP
A
374
−7.221
83.234
20.130
1.00
45.33


ATOM
2095
C
TRP
A
374
−7.675
82.538
21.417
1.00
45.68


ATOM
2096
O
TRP
A
374
−8.651
82.604
21.782
1.00
45.67


ATOM
2097
CB
TRP
A
374
−7.281
82.255
18.954
1.00
41.02


ATOM
2098
CG
TRP
A
374
−8.525
81.456
18.941
1.00
41.06


ATOM
2099
CD1
TRP
A
374
−9.706
81.790
18.354
1.00
39.92


ATOM
2100
CD2
TRP
A
374
−8.743
80.202
19.597
1.00
42.91


ATOM
2101
NE1
TRP
A
374
−10.651
80.828
18.606
1.00
38.27


ATOM
2102
CE2
TRP
A
374
−10.085
79.839
19.369
1.00
44.86


ATOM
2103
CE3
TRP
A
374
−7.931
79.348
20.361
1.00
40.55


ATOM
2104
CZ2
TRP
A
374
−10.639
78.655
19.879
1.00
42.33


ATOM
2105
CZ3
TRP
A
374
−8.481
78.174
20.867
1.00
39.52


ATOM
2106
CH2
TRP
A
374
−9.821
77.841
20.622
1.00
41.43


ATOM
2107
N
LEU
A
375
−6.738
81.878
22.097
1.00
42.95


ATOM
2108
CA
LEU
A
375
−7.036
81.174
23.341
1.00
41.42


ATOM
2109
C
LEU
A
375
−7.601
82.156
24.356
1.00
44.84


ATOM
2110
O
LEU
A
375
−8.787
82.117
24.676
1.00
46.61


ATOM
2111
CB
LEU
A
375
−5.764
80.528
23.907
1.00
36.17


ATOM
2112
CG
LEU
A
375
−5.817
79.160
24.593
1.00
29.33


ATOM
2113
CD1
LEU
A
375
−4.508
78.918
25.292
1.00
26.36


ATOM
2114
CD2
LEU
A
375
−6.945
79.093
25.586
1.00
27.64


ATOM
2115
N
CYS
A
376
−6.743
83.044
24.851
1.00
47.62


ATOM
2116
CA
CYS
A
376
−7.142
34.039
25.838
1.00
48.88


ATOM
2117
C
CYS
A
376
−8.426
84.771
25.466
1.00
47.94


ATOM
2118
O
CYS
A
376
−9.257
85.058
26.327
1.00
47.20


ATOM
2119
CB
CYS
A
376
−6.005
85.024
26.044
1.00
50.29


ATOM
2120
SG
CYS
A
376
−4.439
84.174
26.290
1.00
58.98


ATOM
2121
N
SER
A
377
−8.594
85.073
24.187
1.00
47.38


ATOM
2122
CA
SER
A
377
−9.809
85.739
23.743
1.00
49.18


ATOM
2123
C
SER
A
377
−11.00
84.881
24.160
1.00
49.87


ATOM
2124
O
SER
A
377
−11.903
85.345
24.854
1.00
51.63


ATOM
2125
CB
SER
A
377
−9.812
85.883
22.223
1.00
49.86


ATOM
2126
OG
SER
A
377
−9.123
87.047
21.816
1.00
52.08


ATOM
2127
N
THR
A
378
−10.979
83.622
23.734
1.00
49.22


ATOM
2128
CA
THR
A
378
−12.044
82.671
24.027
1.00
47.64


ATOM
2129
C
THR
A
378
−12.031
82.179
25.472
1.00
49.13


ATOM
2130
O
THR
A
378
−13.041
82.244
26.170
1.00
46.46


ATOM
2131
CB
THR
A
378
−11.949
81.445
23.104
1.00
45.88


ATOM
2132
OG1
THR
A
378
−11.187
81.778
21.940
1.00
45.49


ATOM
2133
CG2
THR
A
378
−13.328
80.992
22.632
1.00
43.26


ATOM
2134
N
ILE
A
379
−10.885
81.669
25.910
1.00
53.40


ATOM
2135
CA
ILE
A
379
−10.727
81.157
27.270
1.00
56.16


ATOM
2136
C
ILE
A
379
−10.876
82.288
28.236
1.00
59.83


ATOM
2137
O
ILE
A
379
−11.090
82.049
29.472
1.00
62.28


ATOM
2138
CB
ILE
A
379
−9.237
80.499
27.446
1.00
54.13


ATOM
2139
CG1
ILE
A
379
−9.228
79.818
28.803
1.00
50.70


ATOM
2140
CG2
ILE
A
379
−8.254
81.547
27.355
1.00
57.43


ATOM
2141
CD1
ILE
A
379
−7.831
79.309
29.103
1.00
49.28


ATOM
2142
N
GLY
A
380
−10.766
83.525
27.808
1.00
62.15


ATOM
2143
CA
GLY
A
380
−10.887
84.668
28.690
1.00
61.36


ATOM
2144
C
CLY
A
380
−9.650
84.862
29.547
1.00
63.54


ATOM
2145
O
GLY
A
380
−9.754
85.048
30.756
1.00
61.23


ATOM
2145
N
LEU
A
381
−8.477
84.809
28.926
1.00
66.75


ATOM
2147
CA
LEU
A
381
−7.224
84.991
29.652
1.30
69.61


ATOM
2148
C
LEU
A
381
−6.675
66.389
29.378
1.00
72.24


ATOM
2149
O
LEU
A
381
−5.508
86.682
29.648
1.00
71.50


ATOM
2150
CB
LEU
A
381
−6.206
83.929
29.219
1.00
70.68


ATOM
2151
CG
LEU
A
381
−6.216
82.609
29.997
1.00
70.44


ATOM
2152
CD1
LEU
A
381
−5.306
81.602
29.306
1.00
70.05


ATOM
2153
CD2
LEU
A
381
−5.762
82.851
31.431
1.00
68.57


ATOM
2154
N
ASN
A
382
−7.539
87.249
28.843
1.00
75.49


ATOM
2155
CA
ASN
A
382
−7.183
88.628
28.521
1.00
76.77


ATOM
2156
CB
ASN
A
382
−7.275
88.851
27.005
1.00
75.92


ATOM
2157
C
ASN
A
382
−8.099
89.609
29.262
1.00
76.77


ATOM
2158
O
ASN
A
382
−8.574
89.260
30.366
1.00
75.18


ATOM
2159
N
GLN
A
383
−8.328
90.720
28.727
1.00
76.77


END















In each of tables 1-4, the columns, marked A-J, indicate the following data:


A: atom number


B: atom identity


C: amino acid identity


D: polypeptide chain


E: MEK1 residue number


F: X coordinate


G: Y coordinate


H: Z coordinate


I: occupancy factor


J: temperature factor













TABLE 2





Structural Coordinate of MEK1/N35/NKFCdel(corresponding to amino acids 24-373


of SEQ ID NO: 2)-compound 1-ATPγS Ternary Complex.

























ATOM
1
N
GLU
A
38
11.151
66.442
12.859
1.00
71.47


ATOM
2
CA
GLU
A
38
9.979
66.846
13.630
1.00
71.26


ATOM
3
C
GLU
A
38
10.272
66.918
15.126
1.00
74.81


ATOM
4
O
GLU
A
38
9.437
67.372
15.905
1.00
74.50


ATOM
5
CB
GLU
A
38
8.797
65.898
13.364
1.00
72.56


ATOM
6
CG
GLU
A
38
9.092
64.428
13.649
1.00
80.22


ATOM
7
CD
GLU
A
38
9.300
63.613
12.378
1.00
91.57


ATOM
8
OE1 
GLU
A
38
8.602
62.586
12.202
1.00
75.81


ATOM
9
OE2 
GLU
A
38
10.166
63.993
11.559
1.00
82.37


ATOM
10
N
LEU 
A
39
11.465
66.477
15.521
1.00
71.20


ATOM
11
CA
LEU
A
39
11.858
66.495
16.929
1.00
70.68


ATOM
12
C
LEU
A
39
12.911
67.569
17.241
1.00
73.80


ATOM
13
O
LEU
A
39
13.365
67.693
18.382
1.00
72.92


ATOM
14
CB
LEU
A
39
12.318
65.108
17.392
1.00
70.67


ATOM
15
CC
LEU
A
39
11.204
64.052
17.541
1.00
75.24


ATOM
16
CD1
LEU
A
39
11.738
62.721
18.044
1.00
75.17


ATOM
17
CD2
LEU
A
39
10.075
64.548
18.439
1.00
77.96


ATOM
18
N
GLU
A
40
13.272
68.359
16.227
1.00
70.35


ATOM
19
CA
GLU
A
40
14.228
69.455
16.404
1.00
69.93


ATOM
20
C
GLU
A
40
13.529
70.622
17.097
1.00
72.11


ATOM
21
O
GLU
A
40
12.436
71.023
16.701
1.00
71.83


ATOM
22
CB
GLU
A
40
14.775
69.926
15.057
1.00
71.49


ATOM
23
CG
GLU
A
40
15.051
68.827
14.059
1.00
83.83


ATOM
24
CD
GLU
A
40
15.611
69.367
12.753
1.00
107.19


ATOM
25
OE1 
GLU
A
40
15.046
70.349
12.224
1.00
104.41


ATOM
26
OE2 
GLU
A
40
16.632
68.829
12.272
1.00
101.92


ATOM
27
N
LEU
A
41
14.166
71.171
18.119
1.00
67.32


ATOM
28
CA
LEU
A
41
13.576
72.256
18.887
1.00
66.62


ATOM
29
C
LEU
A
41
13.832
73.646
18.328
1.00
69.24


ATOM
30
O
LEU
A
41
14.865
73.910
17.722
1.00
68.43


ATOM
31
CB
LEU
A
41
14.035
72.190
20.342
1.00
66.65


ATOM
32
CG
LEU
A
41
13.683
70.913
21.110
1.00
71.10


ATOM
33
CD1
LEU
A
41
13.207
71.256
22.505
1.00
70.93


ATOM
34
CD2
LEU
A
41
12.628
70.112
20.355
1.00
73.92


ATOM
35
N
ASP
A
42
12.884
74.538
18.572
1.00
65.54


ATOM
36
CA
ASP
A
42
13.002
75.927
18.171
1.00
65.17


ATOM
37
C
ASP
A
42
13.993
76.571
19.130
1.00
66.66


ATOM
38
O
ASP
A
42
14.371
75.966
20.134
1.00
66.35


ATOM
39
CB
ASP
A
42
11.643
76.613
18.331
1.00
67.35


ATOM
40
CC
ASP
A
42
11.496
77.821
17.463
1.00
80.52


ATOM
41
OD1
ASP
A
42
10.378
76.044
16.953
1.00
81.98


ATOM
42
OD2
ASP
A
42
12.483
78.583
17.333
1.00
88.08


ATOM
43
N
GLU
A
43
14.400
77.797
18.841
1.00
61.22


ATOM
44
CA
GLU
A
43
15.297
78.504
19.734
1.00 
60.20


ATOM
45
C
GLU
A
43
14.512
76.834
20.997
1.00
61.29


ATOM
46
O
GLU
A
43
14.939
78.530
22.106
1.00
60.78


ATOM
47
CB
GLU
A
43
15.802
79.796
19.077
1.00
61.67


ATOM
48
CG
GLU
A
43
17.201
79.685
18.485
1.00
73.53


ATOM
49
CD
GLU
A
43
17.983
80.991
18.570
1.00
94.40


ATOM
50
OE1
GLU
A
43
17.412
82.003
19.036
1.00
88.83


ATOM
51
OE2 
GLU
A
43
19.166
81.003
18.158
1.00
84.50


ATOM
52
N
GLN
A
44
13.338
79.418
20.804
1.00
56.05


ATOM
53
CA
GLN
A
44
12.456
79.783
21.900
1.00
55.32


ATOM
54
C
GLN
A
44
11.917
78.559
22.643
1.00
56.71


ATOM
55
O
GLN
A
44
11.570
78.645
23.821
1.00
56.32


ATOM
56
CB
GLN
A
44
11.304
80.646
21.379
1.00
56.67


ATOM
57
CG
GLN
A
44
10.175
80.842
22.365
1.00
67.37


ATOM
58
CD
GLN
A
44
8.844
81.063
21.680
1.00
80.20


ATOM
59
OE1
GLN
A
44
8.362
80.205
20.940
1.00
75.96


ATOM
60
NE2
GLN
A
44
8.247
82.226
21.907
1.00
69.26


ATOM
61
N
GLN
A
45
11.863
77.422
21.956
1.00
51.49


ATOM
62
CA
GLN
A
45
11.397
76.177
22.570
1.00
50.73


ATOM
63
C
GLN
A
45
12.516
75.582
23.424
1.00
55.52


ATOM
64
O
GLN
A
45
12.302
75.188
24.578
1.00
54.87


ATOM
65
CD
GLN
A
45
11.016
75.156
21.489
1.00
51.58


ATOM
66
CG
GLN
A
45
9.735
75.450
20.734
1.00
57.34


ATOM
67
CD
GLN
A
45
9.303
74.277
19.860
1.00
69.17


ATOM
68
OE1
GLN
A
45
10.141
73.526
19.342
1.00
61.68


ATOM
69
NE2
GLN
A
45
7.993
74.101
19.703
1.00
59.07


ATOM
70
N
ARG
A
46
13.701
75.476
22.824
1.00
52.52


ATOM
71
CA
ARG
A
46
14.865
74.920
23.494
1.00
52.19


ATOM
72
C
ARG
A
46
15.150
75.702
24.764
1.00
54.56


ATOM
73
O
ARG
A
46
15.510
75.133
25.788
1.00
53.31


ATOM
74
CB
ARG
A
46
16.078
74.976
22.561
1.00
53.75


ATOM
75
CC
ARG
A
46
17.149
73.956
22.878
1.00
67.01


ATOM
76
CD
ARG
A
46
18.506
74.621
23.082
1.00
82.90


ATOM
77
NE
ARG
A
46
18.793
74.864
24.493
1.00
94.74


ATOM
78
CZ
ARG
A
49
18.636
73.960
25.458
1.00
108.67


ATOM
79
NH1
ARG
A
46
18.194
72.741
25.166
1.00
96.82


ATOM
80
NH2
ARG
A
46
18.917
74.276
26.715
1.00
93.20


ATOM
81
N
LYS
A
47
14.942
77.009
24.691
1.00
51.41


ATOM
82
CA
LYS
A
47
15.164
77.890
25.820
1.00
51.49


ATOM
83
C
LYS
A
47
14.115
77.684
26.930
1.00
55.15


ATOM
84
O
LYS
A
47
14.453
77.634
28.117
1.00
54.30


ATOM
85
CB
LYS
A
47
15.169
79.345
25.357
1.00
54.27


ATOM
86
CG
LYS
A
47
14.263
80.252
26.146
1.00
70.16


ATOM
87
CD
LYS
A
47
13.868
81.474
25.307 
1.00
82.24


ATOM
88
CE
LYS
A
47
15.125
82.291
24.927
1.00
94.63


ATOM
89
NZ
LYS
A
47
14.770
83.513
24.241
1.00
105.34


ATOM
90
N
ARG
A
48
12.849
77.562
26.531
1.00
51.89


ATOM
91
CA
ARG
A
48
11.758
77.340
27.473 
1.00 
51.48


ATOM
92
C
ARG
A
48
11.968
76.026
28.213
1.00
54.44


ATOM
93
O
ARG
A
48
11.679
75.920
29.405
1.00
53.22


ATOM
94
CB
ARG
A
48
10.417
77.289
26.736
1.00
52.21


ATOM
95
CG
ARG
A
48
9.871
78.648
26.291
1.00
61.13


ATOM
96
CD
ARG
A
48
8.427
78.496
25.803
1.00
68.19


ATOM
97
NE
ARG
A
48
7.834
79.754
25.352
1.00
71.56


ATOM
98
CZ
ARG
A
48
7.064
79.870
24.272
1.00
78.89


ATOM
99
NH1
ARG
A
48
6.816
78.813
23.511
1.00 
61.26


ATOM
100
NH2
ARG
A
48
6.552
81.044
23.946
1.00
64.80


ATOM
101
N
LEU
A
49
12.458
75.019
27.494
1.00
51.59


ATOM
102
CA
LEU
A
49
12.703
73.708
28.084
1.00
51.83


ATOM
103
C
LEU
A
49
13.874
73.774
29.056
1.00
56.66


ATOM
104
O
LEU
A
49
13.923
73.039
30.045
1.00
55.69


ATOM
105
CB
LEU
A
49
12.984
72.672
26.996
1.00
51.84


ATOM
106
CG
LEU
A
49
12.388
71.273
27.192
1.00
56.92


ATOM
107
CD1
LEU
A
49
12.060
70.998
28.665
1.00
57.19


ATOM
108
CD2
LEU
A
49
11.146
71.086
26.319
1.00
58.69


ATOM
109
N
GLU
A
50
14.828
74.648
28.750
1.00
53.99


ATOM
110
CA
GLU
A
50
16.008
74.820
29.584
1.00
53.94


ATOM
111
C
GLU
A
50
15.600
75.440
30.901
1.00
55.79


ATOM
112
O
GLU
A
50
16.088
75.052
31.959
1.00
55.15


ATOM
113
CB
GLU
A
50
17.038
75.711
28.873
1.00
55.44


ATOM
114
CG
GLU
A
50
18.385
75.802
29.599
1.00
69.06


ATOM
115
CD
GLU
A
50
19.471
76.430
28.731
1.00
94.86


ATOM
116
OE1
GLU
A
50
19.291
76.505
27.498
1.00
89.67


ATOM
117
OE2
GLU
A
50
20.511
76.849
29.294
1.00
91.35


ATOM
118
N
ALA
A
51
14.659
76.378
30.831
1.00
51.27


ATOM
119
CA
ALA
A
51
14.162
77.060
32.014
1.00
50.34


ATOM
120
C
ALA
A
51
13.363
76.131
32.933
1.00
52.94


ATOM
121
O
ALA
A
51
13.541
76.156
34.156
1.00
53.23


ATOM
122
CB
ALA
A
51
13.331
78.260
31.615
1.00
51.19


ATOM
123
N
PHE
A
52
12.491
75.304
32.350
1.00
46.97


ATOM
124
CA
PHE
A
52
11.691
74.383
33.154
1.00
45.85


ATOM
125
C
PHE
A
52
12.575
73.415
33.909
1.00
49.71


ATOM
126
O
PHE
A
52
12.297
73.072
35.055
1.00
49.15


ATOM
127
CB
PHE
A
52
10.664
73.602
32.305
1.00
46.55


ATOM
128
CG
PHE
A
52
9.900
72.559
33.091
1.00
46.83


ATOM
129
CD1
PHE
A
52
8.785
72.913
33.845
1.00
48.58


ATOM
130
CD2
PHE
A
52
10.334
71.241
33.126
1.00
48.60


ATOM
131
CE1
PHE
A
52
8.102
71.967
34.591
1.00
49.11


ATOM
132
CE2
PHE
A
52
9.645
70.282
33.865
1.00
50.89


ATOM
133
CZ
PHE
A
52
8.533
70.648
34.605
1.00
48.55


ATOM
134
N
LEU
A
53
13.630
72.961
33.252
1.00
47.11


ATOM
135
CA
LEU
A
53
14.563
72.021
33.871
1.00
47.57


ATOM
136
C
LEU
A
53
15.323
72.695
35.012
1.00
51.93


ATOM
137
O
LEU
A
53
15.353
72.194
36.132
1.00
51.14


ATOM
138
CB
LEU
A
53
15.530
71.474
32.825
1.00
47.70


ATOM
139
CG
LEU
A
53
14.863
70.618
31.745
1.00
52.34


ATOM
140
CD1
LEU
A
53
15.838
70.308
30.608
1.00
52.65


ATOM
141
CD2
LEU
A
53
14.322
69.334
32.362
1.00
53.88


ATOM
142
N
THR
A
54
15.886
73.863
34.723
1.00
49.89


ATOM
143
CA
THR
A
54
16.624
74.637
35.707
1.00
50.39


ATOM
144
C
THR
A
54
15.797
74.854
36.973
1.00
55.48


ATOM
145
O
THR
A
54
16.302
74.688
38.085
1.00
55.34


ATOM
146
CB
THR
A
54
17.057
75.991
35.130
1.00
58.56


ATOM
147
OG1
THR
A
54
17.811
75.775
33.928
1.00
58.22


ATOM
148
CG2 
THR
A
54
17.912
76.759
36.134
1.00
57.48


ATOM
149
N
GLN
A
55
14.525
75.222
36.805
1.00
52.17


ATOM
150
CA
GLN
A
55
13.638
75.415
37.951
1.00
52.08


ATOM
151
C
GLN
A
55
13.452
74.068
38.620
1.00
56.67


ATOM
152
O
GLN
A
55
13.582
73.938
39.836
1.00
56.46


ATOM
153
CB
GLN
A
55
12.270
75.953
37.511
1.00
53.44


ATOM
154
CG
GLN
A
55
12.286
77.361
36.943
1.00
67.64


ATOM
155
CD
GLN
A
55
10.879 
77.919
36.725
1.00
87.49


ATOM
156
OE1
GLN
A
55
10.073
77.348
35.976
1.00
79.95


ATOM
157
NE2
GLN
A
53
10.572
79.031
37.398
1.00
79.82


ATOM 
158
N
LYS
A
56
13.164
73.060
37.806 
1.00
53.32


ATOM
159
CA
LYS
A
56
12.960
71.706
38.291
1.00
33.07


ATOM
160
C
LYS
A
56
14.093
71.268
39.215
1.00
56.76


ATOM
161
O
LYS
A
56
13.860
70.660
40.250
1.00
56.30


ATOM
162
CB
LYS
A
56
12.849
70.737
37.109
1.00
55.01


ATOM
163
CG
LYS
A
56
12.519
69.314
37.507
1.00
60.46


ATOM
164
CD
LYS
A
56
12.046
68.505
36.309 
1.00
65.81


ATOM
165
CE
LYS
A
56
11.570
67.123
36.732 
1.00
70.78


ATOM
166
NZ
LYS
A
56
10.773
66.467
35.659
1.00
76.04


ATOM
167
N
GLN
A
57
15.317
71.583
38.825
1.00
54.16


ATOM
168
CA
GLN
A
57
16.498
71.192
39.589 
1.00
54.49


ATOM
169
C
GLN
A
57
16.493
71.690
41.033 
1.00
58.36


ATOM
170
O
GLN
A
57
17.030
71.039
41.919
1.00
58.16


ATOM
171
CB
GLN
A
57
17.763
71.665
38.880
1.00
55.99


ATOM
172
CG
GLN
A
57
18.891
70.659
38.889
1.00
72.53


ATOM
173
CD
GLN
A
57
20.110
71.157
38.135 
1.00
94.24


ATOM
174
OE1
GLN
A
57
20.041
72.161
37.417
1.00
87.23


ATOM
175
NE2
GLN
A
57
21.238
70.467
38.303
1.00
88.51


ATOM
176
N
LYS
A
58
15.898
72.853
41.259
1.00
54.90


ATOM
177
CA
LYS
A
58
15.862
73.439
42.594
1.00
54.65


ATOM
178
C
LYS
A
58
14.871
72.750
43.532 
1.00
59.30


ATOM
179
O
LYS
A
58
14.981
72.856
44.759
1.00
58.24


ATOM
180
CB
LYS
A
58
15.554
74.932
42.507 
1.00
56.49


ATOM
181
CG
LYS
A
58
16.509
75.704
41.602 
1.00
60.63


ATOM
192
CD
LYS
A
58
15.996
77.120
41.343
1.00
64.90


ATOM
183
CE
LYS
A
58
16.982
77.922
40.505
1.00
69.91


ATOM
184
NZ
LYS
A
58
16.847
79.391
40.724
1.00
72.05


ATOM
185
N
VAL
A
59
13.907
72.045
42.950
1.00
57.03


ATOM
186
CA
VAL
A
59
12.903
71.326
43.732
1.00
57.20


ATOM
187
C
VAL
A
59
13.519
70.062
44.326
1.00
62.57


ATOM
188
O
VAL
A
59
14.247
69.331
43.646
1.00
62.63


ATOM
189
CB
VAL
A
59
11.670
70.942
42.853
1.00
60.88


ATOM
190
CG1
VAL
A
59
10.546
70.371
43.712
1.00
60.57


ATOM
191
CG2
VAL
A
59
11.176
72.148
42.066
1.00
60.75


ATOM
192
N
GLY
A
60
13.260
69.819
45.598
1.00
59.49


ATOM
193
CA
GLY
A
60
13.813
68.642
46.249
1.00
59.85


ATOM
194
C
GLY
A
60
12.864
67.478
46.072
1.00
64.54


ATOM
195
O
GLY
A
60
12.342
67.255
44.982
1.00
64.49


ATOM
196
N
GLU
A
61
12.627
66.747
47.154
1.00
61.48


ATOM
197
CA
GLU
A
61
11.695
65.632
47.133
1.00
61.14


ATOM
198
C
GLU
A
61
10.316
66.159
47.522 
1.00
64.20


ATOM
199
O
GLU
A
61
10.192
66.959
48.446 
1.00
63.59


ATOM
200
CB
GLU
A
61
12.142
64.546
48.107
1.00
62.63


ATOM
201
CG
GLU
A
61
11.822
63.136
47.647
1.00
73.54


ATOM
202
CD
GLU
A
61
13.073 
62.302
47.425
1.00
92.51


ATOM
203
OE1
GLU
A
61
14.180
62.885
47.394
1.00
90.34


ATOM
204
OE2
GLU
A
61
12.951
61.054
47.283
1.00
80.04


ATOM
205
N
LEU
A
62
9.291
65.742
46.786
1.00
60.20


ATOM
206
CA
LEU
A
62
7.926
66.206
47.032
1.00
59.49


ATOM
207
C
LEU
A
62
7.334 
65.589
48.290
1.00
62.74


ATOM
208
O
LEU
A
52
7.367 
64.380
48.469
1.00
62.60


ATOM
209
CB
LEU
A
62
7.026
65.920
45.816
1.00
59.26


ATOM
210
CG
LEU
A
62
6.903
67.036
44.764
1.00
63.47


ATOM
211
CD1
LEU
A
62
8.118
57.946
44.750
1.00
63.22


ATOM
212
CD2
LEU
A
62
6.642
66.467
43.381
1.00
65.13


ATOM
213
N
LYS
A
63
6.796
66.439
45.161
1.00
58.64


ATOM
214
CA
LYS
A
63
6.195
65.994
50.415
1.00
58.08


ATOM
215
C
LYS
A
63
4.797
66.581
50.525
1.00
60.41


ATOM
216
O
LYS
A
63
4.893
67.763
50.235
1.00
59.38


ATOM
217
CB
LYS
A
63
7.043
66.461
51.611
1.00
60.60


ATOM
218
CG
LYS
A
63
8.212
65.647
51.838
1.00
77.25


ATOM
219
CD
LYS
A
63
8.762
65.718
53.293
1.00
88.58


ATOM
220
CE
LYS
A
63
8.940
64.326
53.898
1.00
99.95


ATOM
221
NZ
LYS
A
63
8.928
64.351
55.392
1.00
109.42


ATOM
222
N
ASP
A
64
3.838
65.754
50.941
1.00
56.62


ATOM
223
CA
ASP
A
64
2.443
66.181
51.043
1.00
56.50


ATOM
224
C
ASP
A
64
2.251
67.535
51.720
1.00
59.47


ATOM
225
O
ASP
A
64
1.646
68.446
51.148
1.00
58.11


ATOM
226
CB
ASP
A
64
1.580
65.118
51.741
1.00
58.61


ATOM
227
CG
ASP
A
64
0.086
65.478
51.735
1.00
72.35


ATOM
228
OD1
ASP
A
64
−0.279
66.510
51.127
1.00
73.31


ATOM
229
OD2
ASP
A
64
−0.717
64.740
52.346
1.00
79.53


ATOM
230
N
ASP
A
65
2.731
67.651
52.952
1.00
55.71


ATOM
231
CA
ASP
A
65
2.558
68.874
53.718
1.00
55.14


ATOM
232
C
ASP
A
65
3.328
70.040
53.114
1.00
58.45


ATOM
233
O
ASP
A
65
3.276
71.154
53.616
1.00
58.17


ATOM
234
CB
ASP
A
65
2.931
68.645
55.185
1.00
57.00


ATOM
235
CG
ASP
A
65
2.642
67.226
55.638
1.00
67.37


ATOM
236
OD1 
ASP
A
65
1.450
66.863
55.771
1.00
67.17


ATOM
237
OD2
ASP
A
65
3.605
66.443
55.775
1.00
76.33


ATOM
238
N
ASP
A
66
4.001
69.787
51.998
1.00
54.77


ATOM
239
CA
ASP
A
66
4.761
70.831
51.315
1.00
54.36


ATOM
240
C
ASP
A
66
3.879
71.638
50.362
1.00
55.88


ATOM
241
O
ASP
A
66
4.344
72.591
49.720
1.00
54.92


ATOM
242
CB
ASP
A
66
5.922
70.208
50.535
1.00
57.02


ATOM
243
CG
ASP
A
66
7.214
70.144
51.351
1.00
71.35


ATOM
244
OD1 
ASP
A
66
7.263
70.746
52.455
1.00
71.32


ATOM
245
OD2
ASP
A
66
8.177
69.499
50.882
1.00
77.25


ATOM
246
N
PHE
A
67
2.607
71.261
50.276
1.00
51.34


ATOM
247
CA
PHE
A
67
1.678
71.904
49.343
1.00
50.36


ATOM
248
C
PHE
A
67
0.521
72.678
49.961
1.00
53.90


ATOM
249
O
PHE
A
67
−0.071
72.264
50.957
1.00
52.58


ATOM
250
CB
PHE
A
67
1.109
70.871
48.369
1.00
51.39


ATOM
251
CG
PHE
A
67
2.139
70.239
47.492
1.00
52.36


ATOM
252
CD1
PHE
A
67
2.639
70.916
46.392
1.00
54.62


ATOM
253
CD2 
PHE
A
67
2.610
68.963
47.762
1.00
54.03


ATOM
254
CE1 
PHE
A
67
3.595
70.338
45.592
1.00
55.20


ATOM
255
CE2 
PHE
A
67
3.562
68.382
46.956
1.00
56.28


ATOM
256
CZ
PHE
A
67
4.054
69.068
45.873
1.00
54.15


ATOM
257
N
GLU
A
68
0.161
73.762
49.290
1.00
50.93


ATOM
258
CA
GLU
A
68
−0.989
74.568
49.645
1.00
51.27


ATOM
259
C
GLU
A
68
−1.935
74.541
48.424
1.00
56.40


ATOM
260
O
GLU
A
68
−1.540
74.911
47.321
1.00
56.15


ATOM
261
CB
GLU
A
68
−0.554
76.007
49.925
1.00
52.56


ATOM
262
CG
GLU
A
68
−1.521
76.793
50.775
1.00
65.06


ATOM
263
CD
GLU
A
68
−1.350
78.295
50.616
1.00
92.76


ATOM
264
OE1
GLU
A
68
−0.287
78.729
50.111
1.00
83.73


ATOM
265
OE2
GLU
A
68
−2.283
79.040
50.991
1.00
91.17


ATOM
266
N
LYS
A
69
−3.155
74.053
48.623
1.00
53.57


ATOM
267
CA
LYS
A
69
−4.143
73.988
47.549
1.00
53.70


ATOM
268
C
LYS
A
69
−4.631
75.394
47.193
1.00
57.76


ATOM
269
O
LYS
A
69
−4.879
76.210
48.078
1.00
57.38


ATOM
270
CB
LYS
A
69
−5.323
73.108
47.973
1.00
56.10


ATOM
271
CG
LYS
A
69
−6.498
72.118
47.009
1.00
71.86


ATOM
272
CD
LYS
A
69
−7.621
72.218
47.506
1.00
82.45


ATOM
273
CE
LYS
A
69
−8.989
72.811
47.193
1.00
95.67


ATOM
274
NZ
LYS
A
69
−10.094
72.020
47.816
1.00
104.79


ATOM
275
N
ILE
A
70
−4.722
75.688
45.896
1.00
54.36


ATOM
276
CA
ILE
A
70
−5.183
77.001
45.443
1.00
54.13


ATOM
277
C
ILE
A
70
−6.599
76.921
44.880
1.00
58.49


ATOM
278
O
ILE
A
70
−7.365
77.574
44.964
1.00
59.71


ATOM
279
CB
ILE
A
70
−4.283
77.585
44.358
1.00
57.17


ATOM
280
CG1
ILE
A
70
−2.835
77.682
44.834
1.00
57.03


ATOM
281
CG2
ILE
A
70
−4.798
78.958
43.921
1.00
58.42


ATOM
282
CD1
ILE
A
70
−1.390
78.223
43.775
1.00
52.96


ATOM
283
N
SER
A
71
−6.921
75.796
44.265
1.00
54.70


ATOM
284
CA
SER
A
71
−8.244
75.603
43.678
1.00
54.05


ATOM
285
C
SER
A
71
−8.312
74.282
42.943
1.00
57.67


ATOM
286
O
SER
A
71
−7.286
73.676
42.640
1.00
57.37


ATOM
287
CB
SER
A
71
−8.592
76.746
42.723
1.00
56.66


ATOM
288
OG
SER
A
71
−7.465
77.159
41.973
1.00
62.55


ATOM
289
N
GLU
A
72
−9.525
73.830
42.665
1.00
54.04


ATOM
290
CA
GLU
A
72
−9.722
72.580
41.952
1.00
53.48


ATOM
291
C
GLU
A
72
−9.705
72.831
40.448
1.00
55.39


ATOM
292
O
GLU
A
72
−10.418
73.697
39.954
1.00
54.01


ATOM
293
CB
GLU
A
72
−11.034
71.927
42.368
1.00
55.03


ATOM
294
CG
GLU
A
72
−10.994
70.405
42.350
1.00
67.69


ATOM
295
CD
GLU
A
72
−12.044
69.767
43.242
1.00
89.57


ATOM
296
OE1
GLU
A
72
−12.560
70.497
44.136
1.00
83.97


ATOM
297
OE2
GLU
A
72
−12.349
68.590
43.058
1.00
84.34


ATOM
298
N 
LEU
A
73
−8.858
72.095
39.732
1.00
51.15


ATOM
299
CA
LEU
A
73
−6.751
72.254
38.279
1.00
50.83


ATOM
300
C
LEU
A
73
−9.713
71.327
37.532
1.00
56.67


ATOM
301
O
LEU
A
73
−9.931
71.489
36.334
1.00
56.84


ATOM
302
CB
LEU
A
73
−7.315
72.016
37.804 
1.00
50.19


ATOM
303
CG
LEU
A
73
−6.271
73.035
38.282
1.00
53.78


ATOM
304
CD1
LEU
A
73
−4.869
72.559
37.969
1.00
52.96


ATOM
305
CD2
LEU
A
73
−6.535
74.401
37.664
1.00
56.11


ATOM
306
N
GLY
A
74
−10.270
70.352
38.246
1.00
54.08


ATOM
307
CA
GLY
A
74
−11.205
69.407
37.660
1.00
54.67


ATOM
308
C
GLY
A
74
−11.002
68.012
38.235
1.00
61.20


ATOM
309
O
GLY
A
74
−10.197
67.816
39.158
1.00
61.09


ATOM
310
N
ALA
A
75
−11.716
67.040
37.678
1.00
59.00


ATOM
311
CA
ALA
A
75
−11.612
65.663
38.139
1.00
59.55


ATOM
312
C
ALA
A
75
−12.138
64.687
37.106
1.00
64.83


ATOM
313
O
ALA
A
75
−13.017
65.012
36.319
1.00
64.68


ATOM
314
CB
ALA
A
75
−12.356
65.487
39.456
1.00
60.31


ATOM
315
N
GLY
A
76
−11.601
63.479
37.123
1.00
62.65


ATOM
316
CA
GLY
A
76
−12.040
62.442
36.222
1.00
63.16


ATOM
317
C
GLY
A
76
−12.873
61.455
37.020
1.00
69.19


ATOM
318
O
GLY
A
76
−13.351
61.772
38.113
1.00
69.35


ATOM
319
N
ASN
A
77
−13.019
60.250
36.492
1.00
66.29


ATOM
320
CA
ASN
A
77
−13.799
59.222
37.154
1.00
66.48


ATOM
321
C
ASN
A
77
−12.932
58.375
38.076
1.00
71.09


ATOM
322
O
ASN
A
77
−12.958
57.141
38.019
1.00
71.21


ATOM
323
CB
ASN
A
77
−14.506
58.351
36.117
1.00
67.89


ATOM
324
CG
ASN
A
77
−15.378
59.167
35.174
1.00
93.31


ATOM
325
OD1
ASN
A
77
−15.236
59.087
33.955
1.00
89.21


ATOM
326
ND2
ASN
A
77
−16.242
60.005
35.743
1.00
84.25


ATOM
327
N
GLY
A
78
−12.172
59.045
38.935
1.00
67.17


ATOM
328
CA
GLY
A
78
−13.301
58.356
39.878
1.00
66.51


ATOM
329
C
GLY
A
78
−9.998
59.110
40.077
1.00
68.27


ATOM
330
O
GLY
A
78
−8.957
58.510
40.343
1.00
68.07


ATOM
331
N
GLY
A
79
−10.063
60.429
39.955
1.00
63.03


ATOM
332
CA
GLY
A
79
−8.890
61.272
40.129
1.00
61.63


ATOM
333
C
GLY
A
79
−9.273
62.745
40.120
1.00
62.16


ATOM
334
O
GLY
A
79
−10.093
63.179
39.317
1.00
62.00


ATOM
335
N
VAL
A
80
−8.682
53.507
41.031
1.00
55.63


ATOM
336
CA
VAL
A
80
−8.953
64.933
41.113
1.00
53.59


ATOM
337
C
VAL
A
80
−7.656
65.664
40.827
1.00
53.85


ATOM
338
O
VAL
A
80
−6.569
65.113
41.026
1.00
53.30


ATOM
339
CE
VAL
A
80
−9.449
65.328
42.512
1.00
57.25


ATOM
340
CG1
VAL
A
80
−9.959
66.756
42.523
1.00
56.77


ATOM
341
CG2
VAL
A
80
−10.515
64.350
42.983
1.90 
57.19


ATOM
342 
N
VAL
A
81
−7.767
66.894
40.335
1.00
47.51


ATOM
343
CA
VAL
A
81
−5.591
67.695
40.036
1.00
45.52


ATOM
344
C
VAL
A
81
−6.717
69.072
40.651
1.00
46.51


ATOM
345
O
VAL
A
81
−7.703
69.772
40.436
1.00
45.51


ATOM
346
CB
VAL
A
81
−6.324
67.813
38.503
1.00
48.91


ATOM
347
CG1
VAL
A
81
−5.039
68.597
38.247
1.00
48.34


ATOM
348
CO2 
VAL
A
81
−6.231
66.427
37.862
1.00
48.78


ATOM
349
N
PHE 
A
82
−5.709
69.455
41.425
1.00
42.84


ATOM
350
CA
PHE 
A
82
−5.698
70.760
42.078
1.00
41.96


ATOM
351
C
PRE 
A
82
−4.591
71.660
41.567
1.00
43.01


ATOM
352
O
PHE 
A
82
−3.503
71.205
41.253
1.00
42.62


ATOM
353
CB
PHE 
A
82
−5.537
70.595
43.601
1.00
43.97


ATOM
354
CG
PHE 
A
82
−6.756
70.043
44.284
1.00
45.99


ATOM
355
CO1 
PHE 
A
82
−6.951
68.678
44.380 
1.00
49.15


ATOM
356
OD2
PHE 
A
82
−7.715
70.894
44.822
1.00
48.15


ATOM
357
OE1
PHE 
A
82
−8.080
68.166
45.006
1.00
50.14


ATOM
358
CE2 
PHE 
A
82
−8.851
70.387
45.439
1.00
50.93


ATOM
359
CZ
PHE 
A
82
−9.030
69.025
45.534
1.00
49.08


ATOM
360
N
LYS
A
83
−4.856
72.950
41.544
1.00
38.85


ATOM
361
CA
LYS
A
83
−3.820
73.918
41.245
1.00
39.03


ATOM
362
C
LYS
A
83
−3.195
74.195
42.628
1.00
45.02


ATOM
363
O
LYS
A
83
−3.878
74.683
43.533
1.00
45.41


ATOM
364
CB
LYS
A
83
−4.424
75.204
40.685
1.00
40.16


ATOM
365
CG
LYS
A
83
−3.394
76.283
40.388
1.00
44.84


ATOM
366
CO
LYS
A
83
−4.064
77.598
40.050
1.00
51.85


ATOM
367
CE
LYS
A
83
−3.058
78.613
39.555
1.00
56.51


ATOM
368 
NZ
LYS
A
83
−3.672
79.962
39.407
1.00
62.92


ATOM
369
N
VAL
A
84
−1.938
73.795
42.813
1.00
41.30


ATOM
370
CA
VAL
A
84
−1.272 
73.933
44.115
1.00
40.08


ATOM
371
C
VAL
A
84
−0.027
74.794
44.073
1.00
44.31


ATOM
372
O
VAL
A
84
0.614
74.954
43.028
1.00
43.05


ATOM
373
CB
VAL
A
84
−0.816
72.554
44.660
1.00
42.76


ATOM
374
CG1
VAL
A
84
−1.998
71.643
44.900
1.00
42.17


ATOM
375
CG2
VAL
A
84
0.180
71.916
43.703
1.00
42.22


ATOM
376
N
SER
A
85
0.359
75.285
45.242
1.00
41.89


ATOM
377
CA
SER
A
85
1.601
76.021
45.378
1.00
41.78


ATOM
378
C
SER
A
85
2.560
75.147
46.163
1.00
44.85


ATOM
379
O
SER
A
85
2.199
74.604
47.210
1.00
43.95


ATOM
380
CB
SER
A
85
1.384
77.332
46.141
1.00
45.56


ATOM
381
OG
SER
A
85
2.630
77.857
46.593
1.00
51.12


ATOM
382
N
HIS
A
86
3.764
74.967
45.640
1.00
41.50


ATOM
383
CA
HIS
A
86
4.775
74.218
46.365
1.00
41.09


ATOM
384
C
HIS
A
86
5.511
75.240
47.246
1.00
46.14


ATOM
385 
O
HIS
A
86
6.361
76.001
46.767
1.00
45.93


ATOM
386
CB
HIS
A
86
5.748 
73.532
45.421
1.00
41.60


ATOM
387
CG
HIS
A
86
6.683
72.596
46.115
1.00
44.78


ATOM
388
ND1
HIS
A
86
8.039
72.830
46.205
1.00
46.56


ATOM
389
CD2
HIS
A
86
6.446 
71.470
46.827
1.00
46.13


ATOM
390
CE1
HIS
A
86
8.601
71.865
45.909
1.00
45.95


ATOM
391
NE2
HIS
A
66
7.658
71.023
47.292
1.00
46.31


ATOM
392
N
LYS
A
87
5.104 
75.304
48.508
1.00
43.26


ATOM
393
CA
LYS
A
87
5.617
76.293
49.458
1.00
43.38


ATOM
394
C
LYS
A
87
7.106
76.589
49.400
1.00
48.21


ATOM
395
O
LYS
A
87
7.510
77.742
49.232
1.00
48.16


ATOM
396
CB
LYS
A
87
5.200 
75.938
50.885
1.00
45.13


ATOM
397
CG
LYS
A
87
3.697
76.031
51.125
1.00
59.88


ATOM
398
CD
LYS
A
87
3.200
74.852
51.980
1.00
68.23


ATOM
399
CE
LYS
A
87
2.192
75.293
53.002
1.00
74.50


ATOM
400
NZ
LYS
A
87
1.531
74.125
53.651
1.00
83.18


ATOM
401
N
PRO
A
88
7.924
75.562
45.599
1.00
45.00


ATOM
402
CA
PRO
A
88
9.361
75.742
49.650
1.00
44.30


ATOM
403
C
PRO
A
88
9.912
76.459
48.436
1.00
47.89


ATOM
404
O
PRO
A
88
10.538
77.519
48.556
1.00
47.01


ATOM
405
CB
PRO
A
88
9.883
74.313
49.709
1.00
45.59


ATOM
406
CG
PRO
A
88
8.508
73.571
50.406
1.00
49.92


ATOM
407
CD
PRO
A
88
7.529
74.184
49.955
1.00
45.51


ATOM
408
N
SER
A
89
9.700
75.859
47.269
1.00
44.44


ATOM
409
CA
SER
A
89
10.197
76.394
46.007
1.00
43.79


ATOM
410
C
SER
A
89
9.389
77.589
45.540
1.00
47.52


ATOM
411
O
SER
A
89
9.841
78.362
44.703
1.00
46.89


ATOM
412
CB
SER
A
89
10.134
75.300
44.931 
1.00
47.67


ATOM
413
OG
SER
A
89
8.903
74.588
45.007
1.00
54.30


ATOM
414
N
GLY
A
90
8.158
77.699
46.031 
1.00
45.42


ATOM
415
CA
GLY
A
90
7.271
78.785
45.604
1.00
45.56


ATOM
416
C
GLY
A
90
6.706
78.553
44.175
1.00
49.86


ATOM
417
O
GLY
A
90
6.058
79.434
43.604
1.00
49.21


ATOM
418
N
LEU
A
91
6.941
77.368
43.614
1.00
46.88


ATOM
419
CA
LEU
A
91
6.434
77.050
42.263
1.00
46.99


ATOM
420
C
LEU
A
91
4.968
76.601
42.305
1.00
49.83


ATOM
421
O
LEU
A
91
4.583
75.797
43.151
1.00
49.55


ATOM
422
CB
LEU
A
91
7.260
75.929
41.622
1.00
47.07


ATOM
423
CG
LEU
A
91
8.720
76.143
41.211
1.00
51.69


ATOM
424
CD1
LEU
A
91
9.379
74.793
41.036
1.00
52.06


ATOM
425
CD2
LEU
A
91
8.835
76.950
39.929 
1.00
52.54


ATOM
426
N
VAL
A
92
4.163
77.100
41.375 
1.00
46.00


ATOM
427
CA
VAL
A
92
2.777
76.667
41.271
1.00
45.49


ATOM
428
C
VAL
A
92
2.769
75.379
40.431
1.00
47.14


ATOM
429
O
VAL
A
92
3.499
75.267
39.468
1.00
45.80


ATOM
430
CB
VAL
A
92
1.884
77.739
40.600
1.00
49.66


ATOM
431
CG1
VAL
A
92
0.539
77.139
40.168
1.00
49.31


ATOM
432
CG2
VAL
A
92
1.657
78.894
41.549
1.00
49.79


ATOM
433
N
MET
A
93
1.989
74.390
40.858
1.00
42.77


ATOM
434
CA
MET
A
93
1.913
73.118
40.148
1.00
41.64


ATOM
435
C
MET
A
93
0.491
72.637
39.994
1.00
43.77


ATOM
436
O
MET
A
93
−0.419
73.094
40.690 
1.00
42.43


ATOM
437
CB
MET
A
93
2.687
72.035
40.902
1.00
43.58


ATOM
438
CG
MET
A
93
4.186
72.293
41.047
1.00
46.81


ATOM
439
SD
MET
A
93
4.908
71.048
42.112
1.00
50.38


ATOM
440
CE
MET
A
93
6.702
71.513
42.045
1.00
46.93


ATOM
441
N
ALA
A
94
0.330
71.639
39.132
1.00
40.18


ATOM
442
CA
ALA
A
94
−0.934
70.962 
38.952
1.00
40.22


ATOM
443 
C
ALA
A
94
−0.745
69.629
39.652
1.00
43.40


ATOM
444
O
ALA
A
94
0.131
68.849
39.280 
1.00
42.72


ATOM
445
CB
ALA
A
94
−1.216
70.738 
37.440
1.00
41.03


ATOM
446
N
ARG
A
95
−1.518
69.390 
40.703
1.00
39.77


ATOM
447
CA
ARG
A
95
−1.380
68.151 
41.457
1.00
39.25


ATOM
448
C
ARG
A
95
−2.572
67.234
41.283
1.00
44.29


ATOM
449
O
ARG
A
95
−3.702
67.588
41.626 
1.00
43.93


ATOM
450
CB
ARG
A
95
−1.138
68.449 
42.943
1.00
37.69


ATOM
451
CG
ARG
A
95
−1.343
67.247 
43.878
1.00
40.83


ATOM
452
CD
ARG
A
95
−0.985
67.613
45.326 
1.00
40.74


ATOM
453
NE
ARG
A
95
−0.842
66.443
46.181
1.03
53.26


ATOM
454
CZ
ARG
A
95
−0.855
66.479
47.515
1.00
66.15


ATOM
455
NH1
ARG
A
95
−1.013
67.630
48.153
1.00
52.85


ATOM
456
NH2
ARG
A
95
−0.708
65.366 
48.212
1.00
51.47


ATOM
457
N
LYS
A
96
−2.312
66.047
40.750
1.00
42.33


ATOM
458
CA
LYS
A
96
−3.352
65.051 
40.550
1.00
43.00


ATOM
459
C
LYS
A
96
−3.264 
63.967
41.627
1.00
49.05


ATOM
460
O
LYS
A
96
−2.190 
63.429
41.900
1.00
47.43


ATOM
461
CH
LYS
A
96
−3.237 
64.424
39.149
1.00
44.21


ATOM
462
CC
LYS
A
96
−4.111
63.185
38.941
1.00
48.45


ATOM
463
CD
LYS
A
96
−3.920
62.593
37.544
1.00
55.17


ATOM
464
CE
LYS
A
56
−5.013
63.051
36.577
1.00
58.25


ATOM
465
NE
LYS
A
96
−4.825 
62.476
35.156
1.00
56.38


ATOM
466
N
LEU
A
97
−4.406
63.641
42.220
1.00
49.53


ATOM
467
CA
LEU
A
97
−4.460
62.634 
43.268
1.00
50.80


ATOM
468
C
LEU
A
97
−5.328
61.447
42.885
1.00
58.90


ATOM
469
O
LEU
A
97
−6.495
61.607
42.555
1.00
57.90


ATOM
470
CB
LEU
A
97
−4.981
63.251
44.566
1.00
50.71


ATOM
471
CC
LEU
A
97
−4.239
64.486
45.069
1.00
55.32


ATOM
472
CD1
LEU
A
97
−5.041
65.757
44.778
1.00
54.76


ATOM
473
CD2
LEU
A
97
−3.952 
64.348
46.562
1.00
58.25


ATOM
474
N
ILE
A
98
−4.757 
60.252
42.971
1.00
59.52


ATOM
475
CA
ILE
A
98
−5.493
59.030
42.668
1.00
61.19


ATOM
476
C
ILE
A
98
−5.511 
58.119
43.903
1.00
69.28


ATOM
477
O
ILE
A
98
−4.503
57.493
44.238
1.00
68.88


ATOM
478
CB
ILE 
A
98
−4.883 
58.281
41.462
1.00
64.20


ATOM
479
CG1
ILE
A
98
−4.806
59.213
40.248
1.00
64.72


ATOM
480
CG2
ILE
A
98
−5.711
57.051
41.122
1.00
64.58


ATOM
481
CDI
ILE 
A
98
−3.476 
59.173
39.528
1.00
71.59


ATOM
482
N
HIS 
A
99
−6.650
58.080
44.590
1.00
69.01


ATOM
483
CA
HIS 
A
99
−6.787
57.277
45.804
1.00
70.49


ATOM
484
C
HIS 
A
99
−6.705
55.771
45.543
1.00
76.02


ATOM
485
O
HIS 
A
99
−7.270
54.971
46.289
1.00
76.36


ATOM
486
CB
HIS 
A
99
−8.094 
57.630
46.550
1.00
71.81


ATOM
487
CG
HIS 
A
99
−8.041
57.361
48.023
1.00
75.67


ATOM
488
ND1
HIS 
A
99
−7.907
56.091
48.542
1.00
77.65


ATOM
489
CD2
HIS 
A
99
−8.101
58.198
49.087
1.00
77.66


ATOM
490
CE1
HIS 
A
99
−7.884
56.156
49.862
1.00
77.12


ATOM
491
NE2
HIS 
A
99
−8.002
57.423
50.218
1.00
77.45


ATOM
492
N
LEU 
A
100
−5.971
55.392
44.502
1.00
72.85


ATOM
493
CA
LEU
A
100
−5.801
53.987
44.153
1.00
72.65


ATOM
494
C
ASN
A
108
6.855
52.274
43.921
1.00
70.27


ATOM
495
O
ASN 
A
108
7.989
52.154
43.446
1.00
69.82


ATOM
496
N
GLN
A
109
5.957 
51.293
43.907
1.00
66.56


ATOM
497
CA
GLN 
A
109
5.674
50.525
42.696
1.00
66.18


ATOM
498
C
GLN 
A
109
5.426
51.450
41.502
1.00
69.26


ATOM
499
O
GLN
A
109
6.289
51.628
40.638
1.00
68.23


ATOM
500
CS
GLN 
A
109
4.463
49.625
42.915
1.00
67.57


ATOM
501
CC
GLN
A
109
3.678
49.938
44.179
1.00
86.30


ATOM
502
CD
GLN
A
109
2.680
48.854
44.522
1.00
109.60


ATOM
503
OE1
GLN
A
109
1.722
48.621
43.784
1.00
106.27


ATOM
504
NE2
GLN
A
109
2.914
48.162
45.633
1.00
101.55


ATOM
505
N
ILE
A
110
4.235
52.029
41.453
1.00
65.59


ATOM,
505
CA
ILE
A
110
3.906
52.947
40.383 
1.00
64.93


ATOM
507
C
ILE
A
110
4.901
54.105
40.428 
1.00
67.50


ATOM
508
O
ILE
A
110
5.390
54.561
39.389 
1.00
67.15


ATOM
509
CB
ILE
A
110
2.470 
53.471
40.517
1.00
67.98


ATOM
510
CG1
ILE
A
110
1.477
52.301
40.477
1.00
68.14


ATOM
511
CG2
ILE
A
110
2.168 
54.474 
39.412
1.00
68.83


ATOM
512
CD1
ILE
A
110
0.369
52.399
41.496
1.00
72.66


ATOM
513
N
ILE
A
111
5.249 
54.529
41.643
1.00
52.88


ATOM
514
CA
ILE
A
111
6.216 
55.607
41.840
1.00
61.96


ATOM
515
C
ILE
A
111
7.518
55.355
41.074
1.00
64.67


ATOM
516
O
IDE
A
111
8.056
56.258
40.439
1.00
64.37


ATOM
517
CB
ILE
A
111
6.527
55.828
43.339
1.00
64.66


ATOM
518
CG1
ILE
A
111
5.241
56.105
44.111
1.00
64.94


ATOM
519
CG2
ILE
A
111
7.491
56.981
43.521
1.00
64.83


ATOM
520
CD1
ILE
A
111
4.080
56.511
42.236
1.00
71.45


ATOM
521
N
ARG
A
112
8.018
54.124
41.138
1.00
60.56


ATOM
522
CA
ARG
A
112
9.252
53.749
40.434
1.00
60.01


ATOM
523
C
ARG
A
112
9.075
53.932
38.918
1.00
61.95


ATOM
524
O
ARG
A
112
9.936
84.496
38.234
1.00
60.73


ATOM
525
CB
ARG
A
112
9.607
52.280
40.727
1.00
61.23


ATOM
526
CG
ARG
A
112
10.387
52.058
42.018
1.00
75.25


ATOM
527
CD
ARG
A
112
10.686
50.572
42.242
1.00
86.86


ATOM
828
NE
ARG
A
112
12.120
50.320
42.367
1.00
99.93


ATOM
529
CZ
ARG
A
112
12.772
49.362
41.711
1.00
117.35


ATOM
530
NH1
ARG
A
112
12.115
48.556
40.886
1.00
106.81


ATOM
531
NH2
ARG
A
112
14.079
49.204
41.885
1.00
103.98


ATOM
532
N
GLU
A
113
7.969
53.410
38.400
1.00
57.61


ATOM
533
CA
GLU
A
113
7.672
53.513
36.978
1.00
56.88


ATOM
534
C
GLU
A
113
7.501
54.985
36.571
1.00
58.03


ATOM
535
O
GLU
A
113
8.172
55.470
35.656
1.00
57.43


ATOM
536
CB
GLU
A
113
6.411
52.714
36.641
1.00
58.32


ATOM
537
CG
GLU
A
113
6.682
51.273
36.237
1.00
70.27


ATOM
538
CD
GLU
A
113
5.465
50.380
36.402
1.00
93.71


ATOM
539
OE1
GLU
A
113
4.347
50.914
36.566
1.00
86.59


ATOM
540
OE2
GLU
A
113
5.632
49.141
36.364
1.00
90.93


ATOM
541
N
LEU
A
114
6.623
55.691
37.282
1.00
52.34


ATOM
542
CA
LEU
A
114
6.354
57.105
37.008
1.00
50.90


ATOM
543
C
LEU
A
114
7.622
57.960
36.917
1.00
54.43


ATOM
544
O
LEU
A
114
7.622
59.029
36.290
1.00
54.17


ATOM
545
CB
LEU
A
114
5.416
57.677
38.064
1.00
50.31


ATOM
546
CG
LEU
A
114
4.021
57.066
38.100
1.00
54.45


ATOM
547
CD1
LEU
A
114
3.421
57.197
39.485
1.00
54.77


ATOM
548
CD2
LEU
A
114
3.123
57.711
37.043
1.00
55.40


ATOM
549
N
GLN
A
115
8.698
57.498
37.547
1.00
49.94


ATOM
550
CA
GLN
A
115
9.948
58.257
37.565
1.00
49.30


ATOM
551
C
GLN
A
115
10.522
58.502
36.177
1.00
52.16


ATOM
552
O
GLN
A
115
11.423
59.320
36.012
1.00
51.78


ATOM
553
CB
GLN
A
115
10.987
57.586
38.475
1.00
50.79


ATOM
554
CG
GLN
A
115
10.540
57.437
39.921
1.00
56.57


ATOM
555
CD
GLN
A
115
10.234
58.766
40.567
1.00
71.57


ATOM
556
OE1
GLN
A
115
10.977
59.734
40.404
1.00
66.84


ATOM
557
NE2
GLN
A
115
9.128
58.827
41.303
1.00
61.16


ATOM
558
N
VAL
A
116
10.004
57.793
35.181
1.00
48.21


ATOM
559
CA
VAL
A
116
10.476
57.956
33.802
1.00
47.63


ATOM
560
C
VAL
A
116
10.082
59.314
33.199
1.00
49.84


ATOM
561
O
VAL
A
116
10.698
59.777
32.235
1.00
48.76


ATOM
562
CB
VAL
A
116
9.951
56.833
32.886
1.00
51.75


ATOM
563
CG1
VAL
A
116
10.731
56.807
31.575
1.00
51.20


ATOM
564
CG2
VAL
A
116
10.046
55.504
33.590
1.00
51.86


ATOM
565
N
LEU
A
117
9.065
59.943
33.789
1.00
45.80


ATOM
566
CA
LEU
A
117
8.572
61.244
33.335
1.00
45.18


ATOM
567
C
LEU
A
117
9.622
62.329
33.465
1.00
49.20


ATOM
568
O
LEU
A
117
9.517
63.379
32.835
1.00
47.79


ATOM
569
CB
LEU
A
117
7.303
61.640
34.107
1.00
44.76


ATOM
570
CG
LEU
A
117
6.098
60.718
33.909
1.00
48.47


ATOM
571
CD1
LEU
A
117
5.042
60.979
34.954
1.00
47.90


ATOM
572
CD2
LEU
A
117
5.529
60.888
32.495
1.00
49.89


ATOM
573
N
HIS
A
118
10.638
62.074
34.289
1.00
46.44


ATOM
574
CA
HIS
A
118
11.726
63.036
34.478
1.00
45.98


ATOM
575
C
HIS
A
118
12.575
63.069
33.219
1.00
50.81


ATOM
576
O
HIS
A
118
13.314
64.013
32.980
1.00
50.41


ATOM
577
CB
HIS
A
118
12.606
62.628
35.688
1.00
46.50


ATOM
578
CG
HIS
A
118
12.035
63.025
37.016
1.00
49.63


ATOM
579
ND1
HIS
A
118
11.683
62.103
37.982
1.00
51.38


ATOM
580
CD2
HIS
A
118
11.755
64.243
37.540
1.00
50.55


ATOM
581
CE1
HIS
A
118
11.212
62.739
39.041
1.00
50.19


ATOM
582
NE2
HIS
A
118
11.239
64.037
38.797
1.00
50.15


ATOM
583
N
GLU
A
119
12.447
62.025
32.407
1.00
48.36


ATOM
584
CA
GLU
A
119
13.203
61.917
31.164
1.00
48.39


ATOM
585
C
GLU
A
119
12.389
62.398
29.944
1.00
51.49


ATOM
586
O
GLU
A
119
12.929
62.552
28.848
1.00
51.08


ATOM
587
CB
GLU
A
119
13.668
60.471
30.961
1.00
49.86


ATOM
588
CG
GLU
A
119
14.284
59.848
32.210
1.00
63.13


ATOM
589
CD
GLU
A
119
14.625
58.370
32.033
1.00
90.64


ATOM
590
OE1
GLU
A
119
14.308
57.737
30.963
1.00
87.20


ATOM
591
OE2
GLU
A
119
15.227
57.785
32.961
1.00
86.97


ATOM
592
N
CYS
A
120
11.101
62.651
30.149
1.00
47.36


ATOM
593
CA
CYS
A
120
10.228
63.135
29.063
1.00
45.40


ATOM
594
C
CYS
A
120
10.259
64.632
28.980
1.00
49.30


ATOM
595
O
CYS
A
120
9.454
65.305
29.607
1.00
49.60


ATOM
596
CB
CYS
A
120
8.801
62.702
29.307
1.00
46.43


ATOM
597
SG
CYS
A
120
8.620
60.923
29.474
1.00
50.32


ATOM
598
N
ASN
A
121
11.175
65.158
28.189
1.00
44.91


ATOM
599
CA
ASN
A
121
11.330
66.597
28.058
1.00
43.99


ATOM
600
C
ASN
A
121
11.091
67.041
26.635
1.00
44.34


ATOM
601
O
ASN
A
121
11.904
66.810
25.759
1.00
43.55


ATOM
602
CB
ASN
A
121
12.716
67.017
28.542
1.00
47.26


ATOM
603
CG
ASN
A
121
13.039
66.452
29.918
1.00
75.03


ATOM
604
OD1
ASN
A
121
12.450
66.865
30.919
1.00
70.43


ATOM
605
ND2
ASN
A
121
13.871
65.414
29.953
1.00
66.55


ATOM
606
N
SER
A
122
9.931
67.636
26.409
1.00
39.22


ATOM
607
CA
SER
A
122
9.526
68.059
25.081
1.00
37.77


ATOM
608
C
SER
A
122
8.517
69.190
25.184
1.00
39.24


ATOM
609
O
SER
A
122
7.730
69.254
26.128
1.00
38.53


ATOM
610
CB
SER
A
122
8.899
66.873
24.331
1.00
41.01


ATOM
611
OG
SER
A
122
8.121
67.313
23.237
1.00
50.29


ATOM
612
N
PRO
A
123
8.529
70.076
24.201
1.00
34.82


ATOM
613
CA
PRO
A
123
7.587
71.190
24.183
1.00
33.77


ATOM:
614
C
PRO
A
123
6.155
70.688
23.988
1.00
35.43


ATOM
615
O
PRO
A
123
5.205
71.4.51
24.110
1.00
34.02


ATOM
616
CB
PRO
A
123
8.019
72.012
22.949
1.00
35.60


ATOM
617
CG
PRO
A
123
9.408
71.520
22.602
1.00
39.84


ATOM
618
CD
PRO
A
123
9.498
70.119
23.087
1.00
35.07


ATOM
619
N
TYR
A
124
6.017
69.408
23.644
1.00
32.12


ATOM
620
CA
TYR
A
124
4.705
68.824
23.374
1.00
31.85


ATOM
621
C
TYR
A
124
4.269
67.878
24.447
1.00
36.25


ATOM
622
O
TYR
A
124
3.272
67.170
24.297
1.00
36.29


ATOM
623
CB
TYR
A
124
4.688
68.133
22.003
1.00
32.15


ATOM
624
CG
TYR
A
124
5.236
69.017
20.918
1.00
32.54


ATOM
625
CD1
TYR
A
124
4.561
70.154
20.526
1.00
34.26


ATOM
626
CD2
TYR
A
124
6.502
68.789
20.383
1.00
33.13


ATOM
627
CE1
TYR
A
124
5.089
70.999
19.581
1.00
34.96


ATOM
628
CE2
TYR
A
124
7.027
69.617
19.439
1.00
33.49


ATOM
629
CZ
TYR
A
124
6.236
70.729
19.053
1.00
40.28


ATOM
630
OH
TYR
A
124
6.887
71.576
18.134
1.00
42.88


ATOM
631
N
ILE
A
125
4.996
67.889
25.558
1.00
32.51


ATOM
632
CA
ILE
A
125
4.678
67.025
26.695
1.00
31.51


ATOM
633
C
ILE
A
125
4.589
67.857
27.961
1.00
36.57


ATOM
634
O
ILE
A
125
5.424
68.723
28.198
1.00
35.99


ATOM
635
CB
ILE
A
125
5.766
65.931
26.904
1.00
33.73


ATOM
636
CG1
ILE
A
125
5.869
65.008
25.669
1.00
33.43


ATOM
637
CG2
ILE
A
125
5.462
65.126
28.163
1.00
34.20


ATOM
638
CD1
ILE
A
125
4.543
64.568
25.098
1.00
38.55


ATOM
639
N
VAL
A
126
3.549
67.620
28.753
1.00
34.41


ATOM
640
CA
VAL
A
126
3.351
68.366
29.994
1.00
34.70


ATOM
641
C
VAL
A
126
4.521
68.063
30.955
1.00
40.63


ATOM
642
O
VAL
A
126
4.842
66.897
31.195
1.00
40.30


ATOM
643
CB
VAL
A
126
2.011
67.950
30.684
1.00
38.08


ATOM
644
CG1
VAL
A
126
2.003
68.345
32.143
1.00
37.40


ATOM
645
CG2 
VAL
A
126
0.798
68.538
29.938
1.00
37.85


ATOM
646
N
GLY
A
127
5.134
69.116
31.491 
1.00
38.38


ATOM
647
CA
GLY
A
127
6.266
68.974
32.430
1.00
38.45


ATOM
648
C
GLY
A
127
5.898
68.243
33.722
1.00
42.49


ATOM
649
O
GLY
A
127
4.624
68.448
34.282
1.00
42.43


ATOM
650
N
PHE
A
128
6.826
67.418
34.203
1.00
39.12


ATOM
651
CA
PHE
A
128
6.636
66.606
35.408
1.00
39.01


ATOM
652
C
PHE
A
128
7.547
67.090
36.545
1.00
44.65


ATOM
653
O
PHE
A
128
8.745
67.302
36.349
1.00
44.02


ATOM
654
CB
PHE
A
128
6.557
65.136
35.058
1.00
40.69


ATOM
655
CG
PHE
A
128
6.955
64.194
36.229
1.00
42.19


ATOM
656
CD1
PHE
A
128
5.780
63.877
36.883
1.00
45.30


ATOM
657
CD2
PHE
A
128
8.123
63.524
36.594
1.00
44.63


ATOM
658
CE1
PHE
A
128
5.775
62.969
37.930
1.00
46.36


ATOM
659
CE2
PHE
A
128
8.126
62.616
37.631
1.00
47.55


ATOM
660
CZ
PHE
A
128
6.954
62.336
38.302
1.00
46.13


ATOM
661
N
TYR
A
129
6.984
67.230
37.739
1.00
42.34


ATOM
662
CA
TYR
A
129
7.773
67.642
38.897
1.00
42.42


ATOM
663
C
TYR
A
129
8.155
66.464
39.787
1.00
48.96


ATOM
664
O
TYR
A
129
9.295
66.367
40.244
1.00
49.29


ATOM
665
CB
TYR
A
129
7.053
68.719
39.692
1.00
42.35


ATOM
666
CG
TYR
A
129
7.217
70.061
39.069
1.00
42.74


ATOM
667
CD1
TYR
A
129
8.476
70.590
38.875
1.00
44.30


ATOM
668
CD2
TYR
A
129
6.122
70.758
38.572
1.00
43.13


ATOM
669
OE1
TYR
A
129
6.650
71.798
38.267
1.00
44.97


ATOM
670
CE2 
TYR
A
129
6.286
71.976
37.970
1.00
44.18


ATOM
671
CZ
TYR
A
129
7.559
72.492
37.814
1.00
51.17


ATOM
672
OH
TYR
A
129
7.745
73.710
37.198
1.00
52.35


ATOM
673
N
GLY
A
130
7.217
65.549
40.003
1.00
46.04


ATOM
674
CA
GLY
A
130
7.497
64.381
40.830
1.00
46.08


ATOM
675
C
GLY
A
130
6.226
63.632
41.192
1.00
50.62


ATOM
676
O
GLY
A
130
5.120
64.072
40.87.6
1.00
49.50


ATOM
677
N
ALA
A
131
6.403
62.488
41.848
1.00
48.50


ATOM
678
CA
ALA
A
131
5.292
61.644
42.274
1.00
49.21


ATOM
679
C
ALA
A
131
5.595
61.028
43.643
1.00
55.41


ATOM
680
O
ALA
A
131
6.708
60.566
43.896
1.00
55.14


ATOM
681
CB
ALA
A
131
5.041
60.539
41.243
1.00
49.77


ATOM
682
N
PHE
A
132
4.596
61.010
44.512
1.00
53.35


ATOM
683
CA
PHE
A
132
4.758
60.439
45.837
1.00
53.84


ATOM
684
C
PHE
A
132
2.430
59.876
46.293
1.00
61.83


ATOM
685
O
PHE
A
132
2.381
60.201
45.728
1.00
61.53


ATOM
686
CB
PHE
A
132
5.257
61.501
46.829
1.00
54.84


ATOM
687
CG
PHE
A
132
4.371
62.709
46.918
1.00
55.48


ATOM
688
CD1
PHE
A
132
4.552
63.782
46.064
1.00
57.76


ATOM
689
CD2
PHE
A
132
3.340
62.762
47.841
1.00
57.07


ATOM
690
CE1
PHE
A
132
3.734
64.885
46.138
1.00
58.13


ATOM
691
CE2
PHE
A
132
2.526
63.871
47.922
1.00
59.31


ATOM
692
CZ
PHE
A
132
2.730
64.935
47.072
1.00
57.20


ATOM
693
N
TYR
A
133
3.476
59.017
47.305
1.00
60.80


ATOM
694
CA
TYR
A
133
2.267
58.398
47.830
1.00
61.84


ATOM
695
C
TYR
A
133
1.993
58.894
49.242
1.00
66.74


ATOM
696
O
TYR
A
133
2.922
59.190
49.996
1.00
66.21


ATOM
697
CE
TYR
A
133
2.413
56.876
47.819
1.00
63.68


ATOM
698
CG
TYR
A
133
1.175
56.121
48.237
1.00
66.33


ATOM
699
CD1
TYR
A
133
0.685
56.208
49.536
1.00
68.60


ATOM
700
CD2
TYR
A
133
0.527
55.274
47.346
1.00
67.43


ATOM
701
CE1
TYR
A
133
−0.432
55.479
49.927
1.00
70.23


ATOM
702
CE2
TYR
A
133
−0.585
54.550
47.720
1.00
68.45


ATOM
703
CZ
TYR
A
133
−1.064
54.655
49.011
1.00
77.03


ATOM
704
OH
TYR
A
133
−2.164
53.910
49.375
1.00
78.72


ATOM
705
N
SER
A
134
0.718
59.006
49.590
1.00
64.57


ATOM
706
CA
SER
A
134
0.328
59.500
50.899
1.00
65.24


ATOM
707
C
SER
A 
134
−1.179
59.456
51.054
1.00
71.77


ATOM
708
O
SER
A
134
−1.914
59.538
50.071
1.00
72.09


ATOM
709
CB
SER
A
134
0.827
60.934
51.088
1.00
65.83


ATOM
710
OG
SER
A
134
−0.059
61.674
51.908
1.00
79.12


ATOM
711
N
ASP
A
135
−1.643
59.331
52.294
1.00
69.39


ATOM
712
CA
ASP
A
135
−3.073
59.281
52.565
1.00
69.55


ATOM
713
C
ASP
A
135
−3.739
58.189
51.708
1.00
72.90


ATOM
714
O
ASP
A
135
−4.942
58.232
51.431
1.00
72.74


ATOM
715
CB
ASP
A
135
−3.709
60.653
52.300
1.00
71.83


ATOM
716
CG
ASP
A
135
−5.178
60.702
52.682
1.00
86.76


ATOM
717
OD1
ASP
A
135
−5.480
60.947
53.875
1.00
88.12


ATOM
718
OD2
ASP
A
135
−6.030
60.451
51.794
1.00
93.17


ATOM
719
N
GLY
A
136
−2.943
57.211
51.293
1.00
68.57


ATOM
720
CA
GLY
A
136
−3.449
56.101
50.506
1.00
67.85


ATOM
721
C
GLY
A
136
−3.645
56.463
49.038
1.00
70.79


ATOM
722
O
GLY
A
136
−3.982
55.601
48.216
1.00
70.55


ATOM
723
N
GLU
A
137
−3.434
57.734
48.706
1.00
65.62


ATOM
724
CA
GLU
A
137
−3.610
58.195
47.336
1.00
64.27


ATOM
725
C
GLU
A
137
−2.287
58.589
46.686
1.00
65.60


ATOM
726
O
GLU
A
137
−1.418
59.186
47.329
1.00
65.58


ATOM
727
CB
GLU
A
137
−4.604
59.360
47.283
1.00
65.51


ATOM
728
CG
GLU
A
137
−4.348
60.440
48.310
1.00
74.65


ATOM
729
CD
GLU
A
137
−5.433
61.490
48.320
1.00
91.48


ATOM
730
OE1
GLU
A
137
−6.450
61.295
47.627
1.00
82.91


ATOM
731
OE2
GLU
A
137
−5.274
62.509
49.026
1.00
85.26


ATOM
732
N
ILE
A
138
−2.134
58.249
45.408
1.00
58.97


ATOM
733
CA
ILE
A
138
−0.919
58.587
44.682
1.00
57.28


ATOM
734
C
ILE
A
138
−0.957
60.045
44.250
1.00
57.15


ATOM
735
O
ILE
A 
138
−2.031
60.604
44.004
1.00
56.89


ATOM
736
CB
ILE
A
138
−0.703
57.680
43.461
1.00
60.47


ATOM
737
CG1
ILE
A
138
−0.424
56.245
43.912
1.00
61.09


ATOM
738
CG2
ILE
A
138
0.450
58.188
42.617
1.00
61.10


ATOM
739
CD1
ILE
A
138
0.531
55.496
43.001
1.00
69.83


ATOM
740
N
SER
A
139
0.213
60.674
44.216
1.00
50.20


ATOM
741
CA
SER
A
139
0.316
62.078
43.839
1.00
48.27


ATOM
742
C
SER
A
139
1.243
62.247
42.636 
1.00
48.99


ATOM
743
O
SER
A
139
2.379
61.763
42.635
1.00
48.04


ATOM
744
CB 
SER
A
139
0.833
62.924
45.026
1.00
51.10


ATOM
745
OG
SER
A
139
−0.156
63.842
45.504
1.00
55.23


ATOM
746
N
ILE
A
140
0.747
62.925
41.605
1.00
43.60


ATOM
747
CA
ILE
A
140
1.548
63.226
40.432
1.00
42.39


ATOM
748
C
ILE
A
140
1.481
64.722 
40.212
1.00
45.48


ATOM
749
O
ILE
A
140
0.401
65.290
40.024
1.00
44.30


ATOM
750
CB
ILE
A
140
1.059
62.475
39.170
1.00
45.22


ATOM
751
CG1
ILE
A
140
1.021
60.972
39.430
1.00
45.94


ATOM
752
CG2
ILE
A
140
1.979
62.752
38.004
1.00
44.14


ATOM
753
CD1
ILE
A
140
0.659
60.137
38.189
1.00
52.48


ATOM
754
N
CYS
A
141
2.633
65.365
40.312
1.00
42.45


ATOM
755
CA
CYS
A
141
2.719
66.808
40.195
1.00
41.58


ATOM
756
C
CYS
A
141
3.326
67.180
38.901
1.00
42.65


ATOM
757
O
CYS
A
141
4.343
66.630
38.494
1.00
42.28


ATOM
758
CB
CYS
A
141
3.531
67.389
41.348
1.00
42.31


ATOM
759
SG
CYS
A
141
2.842
66.957
42.967
1.00
46.63


ATOM
760
N
MET
A
142
2.701
68.122
38.226
1.00
36.40


ATOM
761
CA
MET
A
142
3.170
63.483
36.940
1.00
35.61


ATOM
762
C
MET
A
142
3.109
69.959
36.700
1.00
39.09


ATOM
763
O
MET
A
142
2.639
70.742
37.538
1.00
39.11


ATOM
764
CE
MET
A
142
2.360
67.720
35.864
1.00
37.66


ATOM
765
CG
MET
A
142
0.849
67.895
36.034
1.00
40.66


ATOM
766
SD
MET
A
142
−0.151
66.689
35.007
1.00
43.56


ATOM
767
CE
MET
A
142
−1.438
66.228
36.249
1.00
40.23


ATOM
768
N
GLU
A
143
3.601
70.365
35.541
1.00
34.78


ATOM
769
CA
GLU
A
143
3.553
71.733
35.117
1.00
34.21


ATOM
770
C
GLU
A
143
2.071
72.158
35.078
1.00
39.67


ATOM
771
O
GLU
A
143
1.181
71.358
34.653
1.00
39.25


ATOM
772
CB
GLU
A
143
4.169
71.823
33.729
1.00
35.35


ATOM
773
CG
GLU
A
143
3.966
73.117
33.014
1.00
42.71


ATOM
774
CD
GLU
A
143
4.452
73.051
31.594
1.00
48.44


ATOM
775
OE1
GLU
A
143
4.820
71.948
31.136
1.00
39.76


ATOM
776
OE2
GLU
A
143
4.455
74.090
30.929
1.00
45.53


ATOM
777
N
HIS
A
144
1.793
73.374
35.545
1.00
35.00


ATOM
778
CA
HIS
A
144
0.437
73.877
35.544
1.00
34.22


ATOM
779
C
HIS
A
144
0.189
74.548
34.204
1.00
36.94


ATOM
780
O
HIS
A
144
0.950
75.436
33.788
1.00
38.03


ATOM
781
CB
HIS
A
144
0.186
74.882
36.719
1.00
34.36


ATOM
782
CG
HIS
A
144
−1.080
75.686
36.571
1.00
37.13


ATOM
783
ND1
HIS
A
144
−2.338
75.127
36.673
1.00
38.54


ATOM
784
CD2
HIS
A
144
−1.275
76.999
36.306
1.00
38.24


ATOM
785
CE1
HIS
A
144
−3.252
76.062
36.490
1.00
37.46


ATOM
786
NE2
HIS
A
144
−2.634
77.208
36.265
1.00
37.82


ATOM
787
N
MET
A
145
−0.832
74.084
33.499
1.00
30.64


ATOM
788
CA
MET
A
145
−1.177
74.657
32.196
1.00
30.00


ATOM
789
C
MET
A
145
−2.423
75.506
32.389
1.00
36.02


ATOM
790
O
MET
A
145
−3.512
74.984
32.637
1.00
35.96


ATOM
791
CB
MET
A
145
−1.411
73.547
31.164
1.00
31.59


ATOM
792
CG
MET
A
145
−0.201
72.622
30.964
1.00
33.70


ATOM
793
SD
MET
A
145
1.097
73.408
29.974
1.00
37.21


ATOM
794
CE
MET
A
145
0.292
73.463
28.246
1.00
33.23


ATOM
795
N
ASP
A
146
−2.232
76.824
32.376
1.00
34.11


ATOM
796
CA
ASP
A
146
−3.296
77.775
32.687
1.00
34.28


ATOM
797
C
ASP
A
146
−4.439
77.858
31.682
1.00
38.13


ATOM
798
O
ASP
A
146
−5.466
78.477
31.964
1.00
37.87


ATOM
799
CB
ASP
A
146
−2.718
79.163
32.964
1.00
35.92


ATOM
800
CG
ASP
A
146
−2.038
79.761
31.756
1.00
45.46


ATOM
801
OD1
ASP
A
146
−1.947
79.077
30.720
1.00
45.45


ATOM
802
OD2
ASP
A
146
−1.609
80.932
31.834
1.00
51.52


ATOM
803
N
GLY
A
147
−4.270
77.243
30.519
1.00
33.36


ATOM
804
CA
GLY
A
147
−5.325
77.264
29.510
1.00
32.44


ATOM
805
C
GLY
A
147
−6.292
76.104
29.732
1.00
35.57


ATOM
806
O
GLY
A
147
−7.332
76.019
29.081
1.00
35.05


ATOM
807
N
GLY
A
148
−5.924
75.196
30.638
1.00
31.65


ATOM
808
CA
GLY
A
148
−6.747
74.022
30.951
1.00
31.04


ATOM
809
C
GLY
A
148
−6.661
72.964
29.832
1.00
34.50


ATOM
810
O
GLY
A
148
−5.720
72.969
29.032
1.00
33.20


ATOM
811
N
SER
A
149
−7.643
72.063
29.789
1.00
30.59


ATOM
812
CA
SER
A
149
−7.693
71.038
28.743
1.00
30.39


ATOM
813
C
SER
A
149
−8.552
71.494
27.527
1.00
33.24


ATOM
814
O
SER
A
149
−9.281
72.499
27.602
1.00
31.44


ATOM
815
CB
SER.
A
149
−8.194
69.712
29.308
1.00
33.60


ATOM
816
OG
SER
A
149
−9.370
69.900
30.072
1.00
43.68


ATOM
817
N
LEU
A
150
−8.407
70.785
26.403
1.00
29.51


ATOM
813
CA
LEU
A
150
−9.119
71.133
25.166
1.00
28.78


ATOM
819
C
LEU
A
150
−10.608
70.848
25.238
1.00
33.56


ATOM
820
O
LEU
A
150
−11.386
71.424
24.487
1.00
32.42


ATOM
821
CB
LEU
A
150
−8.471
70.469
23.934
1.00
28.25


ATOM
822
CG
LEU
A
150
−7.274
71.24.2
23.351
1.00
32.35


ATOM
823
CD1
LEU
A
150
−6.840
70.694
21.988
1.00
31.53


ATOM
824
CO2
LEU
A
150
−7.569
72.748
23.259
1.00
34.35


ATOM
825
N
ASP
A
151
−11.012
69.972
26.162
1.00
31.81


ATOM
826
CA
ASP
A
151
−12.423 
69.724
26.374
1.00
32.40


ATOM
827
C
ASP
A
151
−13.006
70.941
27.093
1.00
36.08


ATOM
828
O
ASP
A
151
−14.095
71.405
26.765
1.00
35.15


ATOM
829
CB
ASP
A
151
−12.659
68.444
27.190
1.00
34.83


ATOM
830
CG
ASP
A
151
−11.994
68.483
28.552
1.00
48.34


ATOM
831
OD1
ASP
A
151
−12.702
68.320
29.566
1.00 
43.46


ATOM
832
OD2
ASP
A
151
−10.753
68.575
28.604
1.00
57.90


ATOM
833
N
GLN
A
152
−12.232
71.499
28.020
1.00
33.38


ATOM
834
CA
GLN
A
152
−12.659
72.701
28.745
1.00
32.90


ATOM
835
C
GLN
A
152
−12.686
73.888
27.782
1.00
34.75


ATOM
836
O
GLN
A
152
−13.627
74.698
27.785
1.00
35.30


ATOM
837
CB
GLN
A
152
−11.710
72.984
29.923 
1.00
34.29


ATOM
838
CG
GLN
A
152
−11.779
71.967
31.053 
1.00
35.90


ATOM
839
CD
GLN
A
152
−10.712
72.204
32.139 
1.00
53.57


ATOM
840
OE1
GLN
A
152
−9.529
72.447
31.843
1.00
41.46


ATOM
841
NE2
GLN
A
152
−11.120
72.086
33.394
1.00
51.55


ATOM
842
N
VAL
A
153
−11.671
73.967
26.924
1.00
29.66


ATOM
843
CA
VAL
A
153
−11.587
75.029
25.917 
1.00
28.47


ATOM
844
C
VAL
A
153
−12.763
74.953
24.924
1.00
33.52


ATOM
845
O
VAL
A
153
−13.391
75.968
24.604 
1.00
32.52


ATOM
846
CB 
VAL
A
153
−10.253
74.948
25.131
1.00
32.44


ATOM
847
CG1
VAL
A
153
−10.268 
75.929
23.927
1.00
31.72


ATOM
848
CG2
VAL
A
153
−9.061
75.246
26.072
1.00
32.06


ATOM
849
N
LEU
A
154
−13.038
73.748
24.429
1.00
31.24


ATOM
850
CA
LEU
A
154
−14.147
73.524
23.486
1.00
31.41


ATOM
851
C
LEU
A
154
−15.506
73.991
24.067
1.00
37.12


ATOM
852
O
LEU
A
154
−16.262
74.693
23.405
1.00
36.45


ATOM
853
CB
LEU
A
154
−14.235
72.038
23.136
1.00
31.08


ATOM
854
CG
LEU
A
154
−15.275
71.636
22.096
1.00
35.29


ATOM
855
CD1
LEU
A
154
−15.009
72.347
20.776 
1.00
35.01


ATOM
856
CD2
LEU
A
154
−15.299
70.106
21.913 
1.00
36.52


ATOM
857
N
LYS
A
155
−15.815
73.533
25.282 
1.00
35.14


ATOM
858
CA
LYS
A
155
−17.057
73.888
25.972
1.00
35.99


ATOM
859
C
LYS
A
155
−17.262
75.391
25.922 
1.00
42.43


ATOM
860
O
LYS
A
155
−18.371
75.884
25.672
1.00
43.00


ATOM
861
CB
LYS
A
155
−16.979
73.450
27.438
1.00
38.79


ATOM
862
CG
LYS
A
155
−17.879
72.308
27.802
1.00
60.03


ATOM
863
CD
LYS
A
155
−17.441
71.674
29.114 
1.00
72.91


ATOM
864
CE
LYS
A
155
−17.686
70.168
29.110 
1.00
88.91


ATOM
865
NZ
LYS
A
155
−18.553
69.736
30.250
1.00
99.25


ATOM
866
N
LYS
A
156
−16.169
76.113
26.151 
1.00
39.61


ATOM
867
CA
LYS
A
156
−16.153
77.577
26.151
1.00
38.73


ATOM
868
C
LYS
A
156
−16.306
78.148 
24.760
1.00
40.97


ATOM
869
O
LYS
A
156
−17.092
79.062
24.542 
1.00
40.82


ATOM
870
CB
LYS
A
156
−14.822 
73.077
26.750 
1.00
41.18


ATOM
871
CG
LYS
A
156
−14.895
79.452
27.356 
1.00
56.91


ATOM
872
CD
LYS
A
156
−14.679
79.402
28.853 
1.00
64.59


ATOM
873
CE
LYS
A
156
−14.800
80.790
29.469 
1.00
75.51


ATOM
874 
NZ
LYS
A
156
−13.859
80.980
30.610
1.00
85.01


ATOM
875
N
ALA
A
157
−15.518
77.633
23.819 
1.00
35.59


ATOM
876
CA
ALA
A
157
−15.516
78.156
22.459
1.00
34.03


ATOM
877
C
ALA
A
157
−16.739 
77.802
21.604 
1.00
35.42


ATOM
878
O
ALA
A
157
−17.072
78.527
20.678 
1.00
33.60


ATOM
879
CB
ALA
A
157
−14.232
77.755
21.737
1.00
34.37


ATOM
880
N
GLY
A
158
−17.354
76.658
21.876 
1.00
31.75


ATOM
881
CA
GLY
A
158
−18.464
76.173
21.051
1.00
31.72


ATOM
882
C
GLY
A
158
−17.846
75.166 
20.064 
1.00
36.08


ATOM
833
O
GLY
A
158
−18.025
73.958
20.191 
1.00
37.65


ATOM
884
N
ARG
A
159
−17.072
75.680
19.128 
1.00
31.21


ATOM
885
CA
ARG
A
159
−16.300
74.858
18.189 
1.00
30.50


ATOM
886
C
ARG
A
159
−15.002
75.558
17.890
1.00
32.67


ATOM
887
O
ARG
A
159
−14.937
76.804
18.011
1.00
30.88


ATOM
888
CB
ARG
A
159
−17.076
74.534
16.902
1.00
30.08


ATOM
889
CG
ARG
A
159
−17.410
75.707
16.042
1.00
35.69


ATOM
890
CD
ARG
A
159
−18.399
75.273
14.960
1.00
41.83


ATOM
891
NE
ARG
A
159
−18.659
76.336
13.985
1.00
39.93


ATOM
892
CZ
ARG
A
159
−19.671
76.770
13.686
1.00
51.17


ATOM
893
NH1
ARG
A
159
−20.925
76.235
14.280
1.00
47.55


ATOM
894
NH2
ARG
A
159
−20.034
77.724
12.791
1.00
38.32


ATOM
895
N
ILE
A
160
−13.949
74.826
17.604
1.00
28.72


ATOM
896
CA
ILE
A
160
−12.614
75.382
17.384
1.00
27.42


ATOM
897
C
ILE
A
160
−12.264
75.468
15.896
1.00
32.05


ATOM
898
O
ILE
A
160
−12.434
74.498
15.148
1.00
30.84


ATOM
899
CB
ILE
A
160
−11.560
74.549
18.172
1.00
29.58


ATOM
900
CG1
ILE
A
160
−11.963
74.490
19.664
1.00
28.83


ATOM
901
CG2
ILE
A
160
−10.170
75.128
17.992
1.00
29.71


ATOM
902
CD1
ILE
A
160
−11.075
73.569
20.544
1.00
28.36


ATOM
903
N
PRO
A
161
−11.794
76.644
15.465
1.00
28.54


ATOM
904
CA
PRO
A
161
−11.497
76.889
14.036
1.00
26.92


ATOM
905
C
PRO
A
161
−10.440
75.937
13.472
1.00
29.06


ATOM
906
O
PRO
A
161
−9.541
75.521
14.172
1.00
29.17


ATOM
907
CB
PRO
A
161
−10.966
78.341
14.027
1.00
28.31


ATOM
908
CG
PRO
A
161
−11.419
78.927
15.352
1.00
32.56


ATOM
909
CD
PRO
A
161
−11.384
77.772
16.311
1.00
28.33


ATOM
910
N
GLU
A
162
−10.584
75.598
12.194
1.00
25.23


ATOM
911
CA
GLU
A
162
−9.676
74.694
11.496
1.00
24.24


ATOM
912
C
GLU
A
162
−8.192
75.046
11.668
1.00
28.61


ATOM
913
O
GLU
A
162
−7.370
74.173
11.929
1.00
28.78


ATOM
914
CB 
GLU
A
162
−10.035
74.644
10.004
1.00
25.25


ATOM
915
CG
GLU
A
162
−8.959
74.017
9.130
1.00
33.47


ATOM
916
CD
GLU
A
162
−9.457
73.674
7.747
1.00
38.51


ATOM
917
OE1
GLU
A
162
−10.678
73.723
7.522
1.00
28.97


ATOM
918
OE2
GLU
A
162
−8.621
73.415
6.871
1.00
33.16


ATOM
919
N
GLN
A
163
−7.840
76.314
11.480
1.00
26.44


ATOM
920
CA
GLN
A
163
−6.433
76.724
11.595
1.00
27.23


ATOM
921
C
GLN
A
163
−5.915
76.494
12.984
1.00
31.72


ATOM
922
O
GLN
A
163
−4.741
76.135
13.173
1.00
32.09


ATOM
923
CB
GLN
A
163
−6.236
78.190
11.193
1.00
29.17


ATOM
924
CG
GLN
A
163
−6.341
78.435
9.687
1.00
34.22


ATOM
925
CD
GLN
A
163
−5.857
79.819
9.306
1.00
44.36


ATOM
926
OE1
GLN
A
163
−5.684
80.674
10.160
1.00
40.53


ATOM
927
NE2
GLN
A
163
−5.607
80.019
8.035
1.00
36.16


ATOM
928
N
ILE
A
164
−6.784
76.666
13.977
1.00
26.85


ATOM
929
CA
ILE
A
164
−6.363
76.398
15.343
1.00
25.43


ATOM
930
C
ILE
A
164
−6.160
74.902
15.480
1.00
27.59


ATOM
931
O
ILE
A
164
−5.205
74.447
16.109
1.00
27.47


ATOM
932
CB
ILE
A
164
−7.380
76.267
16.371
1.00
28.21


ATOM
933
CG1
ILE
A
164
−7.507
78.399
16.336
1.00
28.25


ATOM
934
CG2
ILE
A
164
−7.005
76.324
17.778
1.00
28.74


ATOM
935
CD1
ILE
A
164
−6.254
79.144
16.833
1.00
32.23


ATOM
936
N
LEU
A
165
−7.042
74.132
14.847
1.00
22.50


ATOM
937
CA
LEU
A
165
−6.929
72.660
14.894
1.00
22.42


ATOM
938
C
LEU
A
165
−5.699
72.139
14.126
1.00
26.23


ATOM
939
O
LEU
A
165
−5.190
71.067
14.414
1.00
25.77


ATOM
940
CB
LEU
A
165
−8.228
72.000
14.437
1.00
22.36


ATOM
941
CG
LEU
A
165
−9.412
72.239
15.400
1.00
25.97


ATOM
942
CD1
LEU
A
165
−10.676
71.581
14.889
1.00
26.34


ATOM
943
CD2
LEU
A
166
−9.072
71.724
16.846
1.00
26.63


ATOM
944
N
GLY
A
166
−5.190
72.952
13.202
1.00
24.87


ATOM
945
CA
GLY
A
166
−3.955
72.635
12.474
1.00
25.00


ATOM
946
C
GLY
A
166
−2.755
72.675
13.439
1.00
30.03


ATOM
947
O
GLY 
A
166
−1.910
71.778
13.417
1.00
30.25


ATOM
948
N
LYS
A
167
−2.710
73.673
14.326 
1.00
26.89


ATOM
949
CA
LYS
A
167
−1.624
73.733
15.337
1.00
27.08


ATOM
950
C
LYS
A
167
−1.787
72.616
16.359
1.00
29.23


ATOM
951
O
LYS
A
167
−0.814
71.999
16.795
1.00
30.05


ATOM
952
CB
LYS
A
167
−1.601
75.102
16.060
1.00
29.84


ATOM
953
CG
LYS
A
167
−1.334
76.275
15.142
1.00
39.22


ATOM
954
CD
LYS
A
167
−0.032
76.088
14.369
1.00
48.58


ATOM
955
CE
LYS
A
167
0.121
77.154
13.269
1.00
52.34


ATOM
956
NZ
LYS
A
167
1.324
76.931
12.425
1.00
54.69


ATOM
957
N
VAL 
A
168
−3.027
72.352
16.751
1.00
24.07


ATOM
958
CA
VAL
A
168
−3.293
71.268
17.693
1.00
22.47


ATOM
959
C
VAL
A
168
−2.838
69.919
17.084 
1.00
26.56


ATOM
960
O
VAL
A
168
−2.232
69.110
17.757
1.00
27.06


ATOM
961
CB
VAL
A
168
−4.816
71.190
18.056
1.00
24.94


ATOM
962
CG1
VAL
A
168
−5.108
69.947
18.852
1.00
24.15


ATOM
963
CG2
VAL
A
168
−5.279
72.480
18.824 
1.00
23.74


ATOM
964
N
SER
A
169
−3.124
69.718
15.804
1.00
23.86


ATOM
965
CA
SER
A
169
−2.730
68.482
15.088 
1.00
23.84


ATOM
966
C
SER
A
169
−1.220
68.314
15.085
1.00
27.80


ATOM
967
O
SER
A
169
−0.706
67.221
15.342
1.00
27.49


ATOM
968
CB
SER
A
169
−3.229
68.523
13.633
1.00
24.75


ATOM
969
OG
SER
A
169
−4.632
68.46.9 
13.570
1.00
29.49


ATOM
970
N
ILE
A
170
−0.511
69.394
14.754
1.00
24.28


ATOM
971
CA
ILE 
A
170
0.950
69.372
14.727
1.00
24.68


ATOM
972
C
ILE
A
170
1.519
68.913
16.102
1.00
30.29


ATOM
973
O
ILE
A
170
2.383
68.040
16.172
1.00
31.21


ATOM
974
CB
ILE
A
170
1.516
70.773
14.361
1.00
28.00


ATOM
975
CG1
ILE
A
170
1.312
71.057
12.876
1.00
28.41


ATOM
976
CG2
ILE
A
170
3.019
70.893
14.746
1.00
28.95


ATOM
977
CD1
ILE
A
170
1.562
72.518
12.496
1.00
35.07


ATOM
978
N
ALA
A
171
1.001
69.502
17.179
1.00
26.18


ATOM
979
CA
ALA
A
171
1.457
69.229
18.539 
1.00
25.26


ATOM
980
C
ALA
A
171
1.229
67.792
18.973 
1.00
31.52


ATOM
981
O
ALA
A
171
2.103
67.155
19.603
1.00
29.89


ATOM
982
CB
ALA
A
171
0.780
70.188
19.514
1.00
25.72


ATOM
983
N
VAL
A
172
0.039
67.286
18.687 
1.00
29.42


ATOM
984
CA
VAL
A
172
−0.282
65.926. 
19.033
1.00
28.86


ATOM
985
C
VAL 
A
172
0.646
64.958
18.299
1.00
34.69


ATOM
986
O
VAL
A
172
1.224
64.069
18.913
1.00
36.18


ATOM
987
CB
VAL
A
172
−1.741
65.598
18.720
1.00
31.75


ATOM
988
CG1
VAL
A
172
−2.026
64.101
18.972
1.00
31.04


ATOM
989
CG2
VAL
A
172
−2.679
66.498
19.573
1.00
30.92


ATOM
990
N
ILE
A
173
0.791
55.131
16.988
1.00
31.26


ATOM
991
CA
ILE
A
173
1.647
64.248
16.214
1.00
31.50


ATOM
992
C
ILE
A
173
3.107
64.316
16.702
1.00
36.09


ATOM
993
O
ILE
A
173
3.785
63.302
16.752
1.00
35.53


ATOM
994
CB
ILE
A
173
1.621
64.569
14.708
1.00
34.79


ATOM
995
CG1
ILE
A
173
0.295
64.136
14.076
1.00
35.01


ATOM
996
CG2
ILE
A
173
2.765
63.841
14.006
1.00
37.69


ATOM
997
CD1
ILE
A
173
−0.005
64.866
12.744
1.00
39.46


ATOM
998
N
LYS
A
174
3.589
65.522
17.002
1.00
32.10


ATOM
999
CA
LYS
A 
174
4.974
65.687
17.475
1.00
32.23


ATOM
1000
C
LYS
A
174
5.133
65.113
18.862
1.00
36.81


ATOM
1001
O
LYS
A
174
6.213
64.429
19.144 
1.00
36.10


ATOM
1002
CB
LYS
A
174
5.410
67.153
17.434
1.00
34.05


ATOM
1003
CG
LYS
A
174
5.580
67.680
16.027
1.00
33.11


ATOM
1004
CD
LYS
A
174
6.372
68.953
16.004
1.00
33.65


ATOM
1005
CE
LYS
A
174
6.424
69.528
14.621
1.00
43.36


ATOM
1006
NZ
LYS
A
174
7.393
70.656
14.539
1.00
53.94


ATOM
1007
N
GLY
A
175
4.125
65.326
19.709
1.00
33.81


ATOM
1008
CA
GLY
A
175
4.128
64.763
21.051
1.00
33.74


ATOM
1009
C
GLY
A
175
4.141
63.225
21.001
1.00
38.15


ATOM
1010
O
GLY
A
175
4.888
62.572
21.746
1.00
39.00


ATOM
1011
N
LEU
A
176
3.310
62.658
20.133
1.00
33.24


ATOM
1012
CA
LEU
A
176
3.246
61.199
19.949
1.00
32.87


ATOM
1013
C
LEU
A
176
4.564
60.669
19.338
1.00
38.82


ATOM
1014
O
LEU
A
176
5.053
59.616
19.716
1.00 
38.51


ATOM
1015
CB
LEU
A
176
2.061
60.817
19.047
1.00
32.30


ATOM
1016
CG
LEU
A
176
0.630
60.947
19.618
1.00
35.72


ATOM
1017
CD1
LEU
A
176
−0.424 
60.445
18.559
1.00
33.90


ATOM
1018
CD2
LEU
A
176
0.511
60.164
20.918
1.00
37.48


ATOM
1019
N
THR
A
177
5.126
61.411
18.394
1.00
37.37


ATOM
1020
CA
THR
A
177
6.393
61.025
17.778
1.00
38.00


ATOM
1021
C
THR
A
177
7.495
61.001
18.843
1.00
43.86


ATOM
1022
O
THR
A
177
8.338
60.110
18.860
1.00
43.84


ATOM
1023
CB
THR
A
177
6.804
62.012
16.679
1.00
43.68


ATOM
1024
OG1
THR
A
177
5.804
62.025
15.653
1.00
44.93


ATOM
1025
CG2
THR
A
177
8.185
61.602
16.054
1.00
39.12


ATOM
1026
N
TYR
A
178
7.477 
61.988
19.730
1.00
41.14


ATOM
1027
CA
TYR
A
178
8.478
62.079
20.779
1.00
41.45


ATOM
1028
C
TYR
A
178
8.401
60.898
21.741
1.00
45.76


ATOM
1029
O
TYR
A
178
9.390
60.222
21.982
1.00
45.74


ATOM
1030
CB
TYR
A
178
8.353
63.397
21.542
1.00
42.61


ATOM
1031
CG
TYR
A
178
9.199
63.423
22.788
1.00
44.33


ATOM
1032
CD1
TYR
A
178
8.694
62.992
23.995
1.00
46.20


ATOM
1033
CD2
TYR
A
178
10.533
63.815
22.740
1.00
45.02


ATOM
1034
CE1
TYR
A
178
9.475
62.981
25.131
1.00
47.44


ATOM
1035
CE2
TYR
A
178
11.315
63.818
23.884
1.00
45.69


ATOM
1036
CZ
TYR
A
178
10.786
63.386
25.062
1.00
52.82


ATOM
1037
OH
TYR
A
178
11.556
63.372
26.188
1.00
57.37


ATOM
1038
N
LEU
A
179
7.221
60.655
22.292
1.00
42.46


ATOM
1039
CA
LEU
A
179
7.039
59.543
23.219
1.00
42.54


ATOM
1040
C
LEU
A
179
7.531
58.233
22.619
1.00
49.79


ATOM
1041
O
LEU
A
179
8.164
57.420
23.303
1.00
49.04


ATOM
1042
CB
LEU
A
179
5.584
59.413
23.627
1.00
42.01


ATOM
1043
CG
LEU
A
179
5.028
60.537
24.508
1.00
46.28


ATOM
1044
CD1
LEU
A
179
3.531
60.517
24.512
1.00
46.00


ATOM
1045
CD2
LEU
A
179
5.570
60.447
25.937
1.00
48.89


ATOM
1046
N
ARG
A
180
7.225
58.026
21.341
1.00
48.77


ATOM
1047
CA
ARG
A
180
7.611
56.805
20.636
1.00
49.26


ATOM
1048
C
ARG
A
180
9.115
56.736
20.391
1.00
53.43


ATOM
1049
O
ARG
A
180
9.778
55.792
20.804
1.00
54.18


ATOM
1050
CB
ARG
A
180
6.873
56.707
19.308
1.00
50.74


ATOM
1051
CG
ARG
A
180
7.052
55.383
18.603
1.00
63.75


ATOM
1052
CD
ARG
A
180
6.316
55.372
17.281
1.00
77.03


ATOM
1053
NE
ARG
A
180
6.732
56.476
16.421
1.00
87.31


ATOM
1054
CZ
ARG
A
180
6.957
56.358
15.116
1.00
98.76


ATOM
1055
NH1
ARG
A
180
6.813
55.178
14.526
1.00
83.85


ATOM
1056
NH2
ARG
A
180
7.330
57.416
14.404
1.00
82.89


ATOM
1057
N
GLU
A
181
9.639
57.736
19.702
1.00
49.05


ATOM
1058
CA
GLU
A
181
11.049
57.786
19.373
1.00
48.37


ATOM
1059
C
GLU
A
181
11.952
57.723
20.594
1.00
52.58


ATOM
1060
O
GLU
A
181
12.813
56.836
20.702
1.00
52.18


ATOM
1061
CB
GLU
A
181
11.360
59.044
18.570
1.00
49.50


ATOM
1062
CG
GLU
A
181
10.892
58.984
17.137
1.00
59.76


ATOM
1063
CD
GLU
A
181
1.1141
57.628
16.502
1.00
80.18


ATOM
1064
OE1
GLU
A
181
10.294
56.723
16.671
1.00
71.86


ATOM
1065
OE2
GLU
A
181
12.195
57.464
15.847
1.00
70.10


ATOM
1066
N
LYS
A
182
11.783
58.685
21.497
1.00
48.08


ATOM
1067
CA
LYS
A
182
12.644
58.790
22.664
1.00
47.13


ATOM
1068
C
LYS
A
182
12.428
57.770
23.757
1.00
51.69


ATOM
1069
O
LYS
A
182
13.378
57.395
24.441
1.00
52.25


ATOM
1070
CB
LYS
A
182
12.603
60.203
23.245
1.00
48.98


ATOM
1071
CG
LYS
A
182
12.886
61.296
22.228
1.00
58.87


ATOM
1072
CD
LYS
A
182
13.910
60.853
21.205
1.00
68.31


ATOM
1073
CE
LYS
A
182
15.328
61.165
21.670
1.00
79.79


ATOM
1074
NZ
LYS
A
182
16.323
60.186
21.139
1.00
88.95


ATOM
1075
N
HIS
A
183
11.186
57.339
23.959
1.00
47.72


ATOM
1075
CA
HIS
A
183
10.894
56.421
25.055
1.00
47.45


ATOM
1077
C
HIS
A
183
10.227
55.112
24.675
1.00
52.40


ATOM
1078
O
HIS
A
183
9.869
54.32:7
25.854
1.00
51.52


ATOM
1079
CB
HIS
A
183
10.081
57.141
26.144
1.00
48.22


ATOM
1080
CG
HIS
A
183
10.654
58.465
26.540
1.00
51.27


ATOM
1081
ND1
HIS
A
183
11.530
58.610
27.594
1.00
52.89


ATOM
1082
CD2
HIS
A
183
10.522
59.693
25.988
1.00
53.10


ATOM
1083
CE1
HIS
A
183
11.900
59.874
27.685
1.00
52.47


ATOM
1084
NE2
HIS
A
183
11.305
60.554
26.721
1.00
52.89


ATOM
1085
N
LYS
A
184.
10.059
54.883
23.373
1.00
50.38


ATOM
1086
CA
LYS
A
184
9.417
53.666
22.867
1.00
51.42


ATOM
1087
C
LYS
A
184
8.145
53.350
23.624
1.00
56.61


ATOM
1088
O
LYS
A
184
8.007
52.271
24.195
1.00
57.17


ATOM
1089
CB
LYS
A
184
10.375
52.461
22.930
1.00
54.85


ATOM
1090
CG
LYS
A
184
11.845
52.809
22.706
1.00
73.17


ATOM
1091
CD
LYS
A
184
12.561
51.724
21.908
1.00
84.76


ATOM
1092
CE
LYS
A
184
12.531
50.382
22.633
1.00
97.00


ATOM
1093
NZ
LYS
A
184
13.120
49.284
21.804
1.00
106.37


ATOM
1094
N
ILE
A
185
7.229
54.312
23.663
1.00
53.12


ATOM
1095
CA
ILE
A
185
5.965
54.131
24.363
1.00
52.31


ATOM
1096
C
ILE
A
185
4.851
54.931
23.702
1.00
53.30


ATOM
1097
O
ILE
A
185
5.087
56.019
23.170
1.00
53.07


ATOM
1098
CB
ILE
A
185
6.084
54.531
25.824
1.00
55.61


ATOM
1099
CG1
ILE
A
185
6.393
56.027
25.946
1.00
55.98


ATOM
1100
CG2
ILE
A
185
7.160
53.699
26.505
1.00
56.50


ATOM
1101
CD1
ILE
A
185
6.857
56.445
27.346
1.00
58.97


ATOM
1102
N
MET
A
186
3.641
54.375
23.719
1.00
46.79


ATOM
1103
CA
MET
A
186
2.498
55.025
23.110
1.00
45.29


ATOM
1104
C
MET
A
186
1.636.
55.658
24.170
1.00
47.26


ATOM
1105
O
MET
A
186
1.695
55.274
25.346
1.00
47.21


ATOM
1106
CB
MET
A
186
1.688
54.041
22.255
1.00
47.44


ATOM
1107
CG
MET
A
186
0.989
52.935
23.023
1.00
50.59


ATOM
1108
SD
MET
A
186
0.026
51.809
21.927
1.00
54.10


ATOM
1109
CE
MET
A
186
−1.608
52.659
21.933
1.00
50.32


ATOM
1110
N
HIS
A
187
0.860
56.658
23.769
1.00
40.91


ATOM
1111
CA
HIS
A
187
0.028
57.387
24.711
1.00
39.05


ATOM
1112
C
HIS
A
187
−1.036
56.509
25.363
1.00
41.20


ATOM
1113
O
HIS
A
187
−1.168
56.493
26.595
1.00
39.69


ATOM
1114
CB
HIS
A
187
−0.625
58.610
24.024
1.00
38.94


ATOM
1115
CG
HIS
A
187
−1.184
59.610
24.985
1.00
41.40


ATOM
1116
ND1
HIS
A
187
−2.213
59.312
25.851
1.00
42.69


ATOM
1117
CD2
HIS
A
187
−0.856
60.905
25.218
1.00
42.00


ATOM
1118
CE1
HIS
A
187
−2.488
60.379
26.584
1.00
41.73


ATOM
1119
NE2
HIS
A
187
−1.677
61.357
26.218
1.00
41.74


ATOM
1120
N
ARG
A
188
−1.825
55.829
24.522
1.00
37.02


ATOM
1121
CA
ARG
A
188
−2.935
54.938
24.974
1.00
36.30


ATOM
1122
C
ARG
A
188
−4.184
55.664
25.390
1.00
40.37


ATOM
1123
O
ARG
A
188
−5.243
55.043
25.502
1.00
39.96


ATOM
1124
CB
ARG
A
188
−2.445
54.031
26.115
1.00
37.24


ATOM
1125
CG
ARG
A
188
−1.555
52.882
25.689
1.00
46.38


ATOM
1126
CD
ARG
A
188
−1.062
52.076
26.903
1.00
54.04


ATOM
1127
NE
ARG
A
188
0.222
51.422
26.627
1.00
63.45


ATOM
1128
CZ
ARG
A
188
0.351
50.290
25.938
1.00
74.87


ATOM
1129
NH1
ARG
A
188
−0.723
49.671
25.466
1.00
53.69


ATOM
1130
NH2
ARG
A
188
1.552
49.772
25.730
1.00
65.85


ATOM
1131
N
ASP
A
189
−4.095
56.965
25.661
1.00
35.99


ATOM
1132
CA
ASP
A
189
−5.287
57.692
25.079
1.00
34.79


ATOM
1133
C
ASP
A
189
−5.386
59.110
25.527
1.00
37.36


ATOM
1134
O
ASP
A
189
−5.606
60.061
26.265
1.00
36.75


ATOM
1135
CB
ASP
A
189
−5.455
57.656
27.611
1.00
35.64


ATOM
1136
CG
ASP
A
189
−6.888
57.987
28.063
1.00
39.81


ATOM
1137
OD1
ASP
A
189
−7.837
57.783
27.282
1.00
37.95


ATOM
1138
OD2
ASP
A
189
−7.057
58.483
29.200
1.00
44.73


ATOM
1139
N
VAL
A
190
−5.299
54.231
24.209
1.00
32.74


ATOM
1140
CA
VAL
A
190
−5.463
60.515
23.563
1.00
31.25


ATOM
1141
C
VAL 
A
190
−6.941
60.892
23.577
1.00
34.54


ATOM
1142
O
VAL
A
190
−7.808
60.063
23.288
1.00
33.71


ATOM
1143
CB
VAL 
A
190
−4.954
60.493
22.087
1.00
34.46


ATOM
1144
CG1
VAL
A
190
−5.315
61.802
21.364
1.00
33.35


ATOM
1145
CG2
VAL
A
190
−3.442
60.248
22.038
1.00
34.32


ATOM
1146
N
LYS
A
191
−7.218
62.141
23.946
1.00
30.06


ATOM
1147
CA
LYS
A
191
−8.574
62.678
23.962
1.00
28.85


ATOM
1148
C
LYS
A
191
−8.477
64.140
24.371
1.00
33.58


ATOM
1149
O
LYS
A
191
−7.431
64.583
24.836
1.00
34.07


ATOM
1150
CB
LYS
A
191
−9.478
61.881
24.897
1.00
29.99


ATOM
1151
CG
LYS
A
191
−9.065
61.918
26.365
1.00
31.44


ATOM
1152
CD
LYS
A
191
−9.861
60.921
27.161
1.00
36.50


ATOM
1153
CE
LYS
A
191
−9.794
61.197
28.648
1.00
43.47


ATOM
1154
NZ
LYS
A
191
−10.123
59.984
29.426
1.00
52.01


ATOM
1155
N
PRO
A
192
−9.530
64.909
24.143
1.00
30.66


ATOM
1156
CA
PRO
A
192
−9.474
66.359
24.433
1.00
29.70


ATOM
1157
C
PRO
A
192
−9.046
66.741
25.850
1.00
31.72


ATOM
1158
O
PRO
A
192
−8.323
67.705
26.035
1.00
32.55


ATOM
1159
CB
PRO
A
192
−10.892
66.847
24.121
1.00
31.08


ATOM
1160
CG
PRO
A
192
−11.449
65.814
23.162
1.00
35.70


ATOM
1161
CD
PRO
A
192
−10.839
64.504
23.580
1.00
31.05


ATOM
1162
N
SER
A
193
−9.483
65.984
26.848
1.00
27.88


ATOM
1163
CA
SER
A
193
−9.124
66.296
28.229
1.00
27.48


ATOM
1164
C
SER
A
193
−7.662
65.953
28.556
1.00
32.42


ATOM
1165
O
SER
A
193
−7.166
66.273
29.650
1.00
30.99


ATOM
1166
CB
SER
A
193
−10.105
65.638
29.228
1.00
29.74


ATOM
1167
OG
SER
A
193
−9.817
64.269
29.431
1.00
31.19


ATOM
1168
N
ASN
A
194
−6.967
65.325
27.595
1.00
29.51


ATOM
1169
CA
ASN
A
194
−5.559
64.942
27.792
1.00
28.95


ATOM
1170
C
ASN
A
194
−4.600
65.748
26.931
1.00
31.70


ATOM
1171
O
ASN
A
194
−3.416
65.441
26.837
1.00
31.39


ATOM
1172
CB
ASN
A
194
−5.356
63.430
27.640
1.00
29.30


ATOM
1173
CC
ASN
A
194
−5.915
62.651
28.825
1.00
43.62


ATOM
1174
OD1
ASN
A
194
−6.294
63.246
29.837
1.00
32.55


ATOM
1175
ND2
ASN
A
194
−6.019
61.326
28.686
1.00
31.52


ATOM
1176
N
ILE
A
195
−5.132
66.794
26.314
1.00
27.16


ATOM
1177
CA
ILE
A
195
−4.339
67.742
25.563
1.00
26.39


ATOM
1178
C
ILE
A
195
−4.497
69.079
26.280
1.00
30.55


ATOM
1179
O
ILE
A
195
−5.603
69.618
26.368
1.00
30.29


ATOM
1180
CB
ILE
A
195
−4.841
67.880
24.109
1.00
28.81


ATOM
1181
CG1
ILE
A
195
−4.916
66.498
23.438
1.00
28.51


ATOM
1182
CG2
ILE
A
195
−3.945
68.813
23.326
1.00
28.01


ATOM
1183
CD1
ILE
A
195
−5.743
66.433
22.151
1.00
29.33


ATOM
1184
N
LEU
A
196
−3.400
69.592
26.829
1.00
28.59


ATOM
1185
CA
LEU
A
196
−3.425
70.849
27.615
1.00
28.18


ATOM
1186
C
LEU
A
196
−2.793
72.001
26.896
1.00
31.40


ATOM
1187
O
LEU
A
196
−1.899
71.813
26.086
1.00
30.46


ATOM
1168
CB
LEU
A
196
−2.764
70.659
28.988
1.00
28.17


ATOM
1189
CG
LEU
A
196
−3.176
69.429
29.788
1.00
33.14


ATOM
1190
CD1
LEU
A
196
−2.545
69.472
31.185
1.00
33.61


ATOM
1191
CD2
LEU
A
196
−4.711
69.310
29.878
1.00
33.60


ATOM
1192
N
VAL
A 
197
−3.287
73.205
27.190
1.00
27.99


ATOM
1193
CA
VAL
A
197
−2.831
74.431
26.534
1.00
28.13


ATOM
1194
C
VAL
A
197
−2.551
75.553
27.564
1.00
33.06


ATOM
1195
O
VAL
A
19.7
−2.980
75.478
23.717
1.00
32.45


ATOM
1196
CB
VAL
A
197
−3.874
74.919
25.456
1.00
32.34


ATOM 
1197
CG1
VAL
A
197
−4.014
73.877
24.329
1.00
32.14


ATOM
1198
CG2
VAL
A
197
−5.246
75.185
26.099
1.00
31.87


ATOM
1199
N
ASN
A
198
−1.760
76.541
27.177
1.00
30.82


ATOM
1200
CA
ASN
A
198
−1.425
77.617
28.114
1.00
30.80


ATOM
1201
C
ASN
A 
198
−1.382
78.960
27.433
1.00
34.26


ATOM
1202
O
ASN
A
198
−1.385
79.039
26.211
1.00
32.21


ATOM
1203
CB
ASN
A
198
−0.111
77.321
28.888
1.00
30.02


ATOM
1204
CG
ASN
A
198
1.126
77.327
27.994
1.00
42.37


ATOM
1205
OD1
ASN
A
198
1.165
77.982
26.959
1.00
39.43


ATOM
1206
ND2 
ASN
A
198
2.161
76.633
28.432
1.00
39.20


ATOM
1207
N
SER
A
199
−1.333
80.026
28.229
1.00
32.55


ATOM
1208
CA
SER
A
199
−1.326
81.392
27.687
1.00
32.79


ATOM
1209
C
SER
A
199
−0.122
81.713
26.803
1.00
38.55


ATOM
1210
O
SER
A
199
−0.153
82.671
26.057
1.00
38.67


ATOM
1211
CB
SER
A 
199
−1.478
82.430
28.802
1.00
36.41


ATOM
1212
OG
SER
A
199
−0.570
82.178
29.867
1.00
45.99


ATOM
1213
N
ARG
A
200
0.932
80.909
26.876
1.00
36.53


ATOM
1214
CA
ARG
A
200
2.093
81.134
26.000
1.00
36.86


ATOM
1215
C
ARG
A
200
1.831
88.571
24.585
1.00
39.52


ATOM
1216
O
ARG
A
200
2.594
80.828
23.650
1.00
38.97


ATOM
1217
CB
ARG
A
200
3.347
80.503
26.587
1.00
37.93


ATOM
1218
CG
ARG
A
200
3.885
81.237
27.771
1.00
50.46


ATOM
1219
CD
ARG
A
200
5.074 
80.529
28.334
1.00
62.70


ATOM
1220
NE
ARG
A
200
6.043
81.468
28.882
1.00
73.77


ATOM
1221
CZ
ARG
A
200
7.241
81.118
29.327
1.00
86.34


ATOM
1222
NH1
ARG
A
200
7.617
79.844
29.289
1.00
68.09


ATOM
1223
NH2
ARG
A
200
8.061
82.038
29.815
1.00
75.00


ATOM
1224
N
GLY
A
201
0.763
79.785
24.448
1.00
34.32


ATOM
1225
CA
GLY
A
201
0.408
79.207
23.150
1.00
33.57


ATOM
1226
C
GLY
A
201
0.977
77.801
22.970
1.00
35.65


ATOM
1227
O
GLY
A
201
1.062
77.295
21.856
1.00
35.59


ATOM
1228
N
GLU
A
202
1.337
77.161
24.072
1.00
30.45


ATOM
1229
CA
GLU
A
202
1.870
75.808
23.999
1.00
29.82


ATOM
1230
C
GLU
A
202
0.726
74.806
24.058
1.00
32.98


ATOM
1231
O
GLU
A
202
−0.336
75.093
24.613
1.00
30.11


ATOM
1232
CB
GLU
A
202
2.880
75.546
25.124
1.00
30.44


ATOM
1233
CG
GLU
A
202
4.024
76.545
25.129
1.00
37.82


ATOM
1234
CD
GLU
A
202
5.034
76.271
26.233
1.00
49.43


ATOM
1235
OE1
GLU
A
202
4.638
76.225
27.421
1.00
36.18


ATOM
1236
OE2
GLU
A
202
6.216
76.082
25.903
1.00
50.68


ATOM
1237
N
ILE
A
203
0.951
73.658
23.432 
1.00
31.00


ATOM
1238
CA
ILE
A
203
−0.030
72.581
23.339
1.00
30.51


ATOM
1239
C
ILE
A
203
0.723
71.302
23.682 
1.00
32.75


ATOM
1240
O
ILE
A
203
1.740
71.015
23.073 
1.00
32.65


ATOM
1241
CB
ILE
A
203
−0.600
72.522
21.679
1.00
33.10


ATOM
1242
CG1
ILE
A
203
−1.125
73.922
21.479
1.00
33.02


ATOM
1243
CG2
ILE
A
203
−1.684
71.448
21.746
1.00
31.97


ATOM
1244
CD1
ILE
A
203
−1.493
74.057
19.999
1.00
32.51


ATOM
1245
N
LYS
A
204
0.288
70.604
24.738
1.00
28.31


ATOM
1246
CA
LYS
A
204
1.027
69.441
25.253
1.00
28.01


ATOM
1247
C
LYS
A
204
0.160
68.311
25.701
1.00
32.56


ATOM
1248
O
LYS
A
204
−0.900
68.525
26.271
1.00
32.29


ATOM
1249
CB
LYS
A
204
1.910
69.856
26.449
1.00
29.78


ATOM
1250
CG
LYS
A
204
2.721
71.126
26.214
1.00
38.47


ATOM
1251
CD
LYS
A
204
3.603
71.443
27.413
1.00
39.97


ATOM
1252
CE
LYS
A
204
4.445
72.673
27.162
1.00
39.62


ATOM
1253
NZ
LYS
A
204
5.365
72.948
28.319
1.00
46.59


ATOM
1254
N
LEU
A
205
0.681
67.096
25.559 
1.00
29.67


ATOM
1255
CA
LEU
A
205
−0.036
65.895
25.969
1.00
29.10


ATOM
1256
C
LEU
A
205
0.289
65.507
27.402
1.00
35.15


ATOM
1257
O
LEU
A
205
1.402
65.719
27.887
1.00
34.87


ATOM
1258
CB
LEU
A
205
0.347
64.730
25.059 
1.00
28.89


ATOM
1259
CG
LEU
A
205
0.169
64.929
23.570
1.00
32.84


ATOM
1260
CD1
LEU
A
205
0.795
63.742
22.811
1.00
32.52


ATOM
1261
CD2
LEU
A
205
−1.308
65.085
23.256
1.00
33.44


ATOM
1252
N
CYS
A
206
−0.675
64.885
28.059
1.00
34.14


ATOM
1263
CA
CYS
A
206
−0.486
64.412
29.412
1.00
35.16


ATOM
1264
C
CYS
A
206
−1.213
63.082
29.579
1.00
38.96


ATOM
1265
O
CYS
A
206
−1.857
62.591
28.638
1.00
37.59


ATOM
1266
CB
CYS 
A
206
−1.018
65.435 
30.416
1.00
36.07


ATOM
1267
SG
CYS
A
206
−2.839
65.538
30.490
1.00
40.38


ATOM
1268
N
ASP
A
207
−1.089
62.492
30.760
1.00
35.92


ATOM
1269
CA
ASP
A
207
−1.778
61.246
31.061
1.00
36.18


ATOM
1270
C
ASP
A
207
−1.497
60.083
30.092
1.00
41.37


ATOM
1271
O
ASP
A
207
−2.362 
59.250
29.866
1.00
40.36


ATOM
1272
CB
ASP
A
207
−3.290
51.489
31.186
1.00
37.56


ATOM
1273
CG
ASP
A
207
−3.639
62.392
32.357
1.00
45.10


ATOM
1274
OD1
ASP
A
207
−2.699
62.906
33.005
1.00
46.10


ATOM
1275
OD2
ASP
A
207
−4.845
62.627
32.606
1.00
47.45


ATOM
1276
N
PHE
A
208
−0.281
60.021
29.550
1.00
40.15


ATOM
1277
CA
PHE
A
208
0.100
58.906
28.687
1.00
41.33


ATOM
1278
C
PHE
A
208
0.585
57.733
29.570
1.00
50.26


ATOM
1279
O
PHE
A
208
0.923
57.928
30.740
1.00
49.46


ATOM
1280
CB
PHE
A
208
1.183
59.307
27.686
1.00
42.36


ATOM
1281
CG
PHE 
A
208
2.186
60.275 
28.228
1.00
43.26


ATOM
1282
CD1
PHE
A
208
3.357
59.824
28.817
1.00
45.42


ATOM
1283
CD2
PHE
A
208
1.976
61.645
28.120
1.00
44.33


ATOM
1284
CE1
PHE
A
208
4.288
60.717
29.300
1.00
45.76


ATOM
1285
CE2
PHE
A
208
2.910
62.544
28.600
1.00
46.52


ATOM
1286
CZ
PHE
A
208
4.067
62.084
29.181
1.00
44.55


ATOM
1287
N
GLY
A
209
0.589
56.526
29.007
1.00
50.61


ATOM
1288
CA
GLY
A
209
0.943
55.312
29.758
1.00
52.34


ATOM
1289
C
GLY
A
209
2.449
55.063
29.901 
1.00
58.83


ATOM
1290
O
GLY
A
209
3.000
54.140
29.292
1.00
57.91


ATOM
1291
N
VAL
A
210
3.098
55.870
30.732 
1.00
57.44


ATOM
1292
CA
VAL
A
210
4.526
55.734 
30.978 
1.00
58.38


ATOM
1293
C
VAL
A
210
4.756
54.695
32.076
1.00
64.19


ATOM
1294
O
VAL
A
210
5.858
54.180 
32.235
1.00
64.05


ATOM
1295
CB
VAL
A
210
5.144
57.084
31.435
1.00
62.40


ATOM
1296
CG1
VAL
A
210
4.901
57.301
32.907
1.00
62.04


ATOM
1297
CG2
VAL
A
210
6.634
57.132
31.125
1.00
62.32


ATOM
1298
N
SFR
A
211
3.700
54.381
32.815
1.00
62.32


ATOM
1299
CA
SER
A
211
3.790
53.424
33.910
1.00
63.27


ATOM
1300
C
SER
A
211
3.553
51.975
33.479
1.00
69.46


ATOM
1301
O
SER
A
211
4.453
51.316
32.939
1.00
69.36


ATOM
1302
CB
SER
A
211
2.825
53.806
35.032
1.00
66.52


ATOM
1303
OG
SER
A
211
3.084
53.056
36.207
1.00
74.95


ATOM
1304
N
GLY
A
212
2.353
51.473
33.755
1.00
66.88


ATOM
1305
CA
GLY
A
212
2.003
50.096
33.432
1.00
57.19


ATOM
1306
C
GLY
A
212
1.194
49.512
34.575
1.00
72.37


ATOM
1307
O
GLY
A
212
0.047
49.101
34.392
1.00
71.80


ATOM
1308
N
GLN
A
213
1.782
49.514
35.767
1.00
70.36


ATOM
1309
CA
GLN
A
213
1.096
49.020
36.951
1.00
70.55


ATOM
1310
C
GLN
A
213
−0.022
49.984
37.331
1.00
76.21


ATOM
1311
O
GLN
A
213
−1.073
49.568
37.829
1.00
76.23


ATOM
1312
CB
GLN
A
213
2.078
48.851
38.114
1.00
72.31


ATOM
1313
CG
GLN
A
213
2.008
47.486
38.792 
1.00
86.28


ATOM
1314
CD
GLN
A
213
0.724
47.291
39.586
1.00
106.04


ATOM
1315
OE1
GLN
A
213
0.342
48.142
40.393
1.00
100.96


ATOM
1316
NE2
GLN
A
213
0.057
46.161
39.356
1.00
42.65


ATOM
1317
N
LEU
A
214
0.203
51.271
37.074 
1.00
73.50


ATOM
1318
CA
LEU
A
214
−0.803
52.290
37.351
1.00
73.43


ATOM
1319
C
LEU
A
214
−1.9.95 
52.078
36.424
1.00
78.06


ATOM
1320
O
LEU
A
214
−3.146
52.318
36.803
1.00
77.39


ATOM
1321
CB
LEU
A
214
−0.219
53.589
37.146
1.00
73.34


ATOM
1322
CG
LEU
A
214
−1.142
54.856
37.505 
1.00
77.65


ATOM
1323
CD1
LEU
A
214
−1.642
54.719
38.936
1.00
77.79


ATOM
1324
CD2
LEU
A
214
−0.442
56.199
37.297
1.00
79.33


ATOM
1325
N
ILE
A
215
−1.712
51.609
35.210
1.00
75.79


ATOM
1326
CA
ILE
A
215
−2.759
51.341
34.231 
1.00
76.34


ATOM
1327
C
ILE
A
215
−3.615
50.171
34.696
1.00
82.06


ATOM
1328
O
ILE
A
215
−4.845
50.217
34.623
1.00
81.87


ATOM
1329
CB
ILE
A
215
−2.174
50.995
32.846
1.00
79.49


ATOM
1330
CG1
ILE
A
215
−1.541
52.232
32.200
1.00
79.73


ATOM
1331
CG2
ILE
A
215
−3.259
50.408
31.942
1.00
80.26


ATOM
1332
CD1
ILE
A
215
−0.255
51.942
31.444
1.00
84.61


ATOM
1333
N
ASP
A
216
−2.952
49.120
35.170
1.00
79.61


ATOM
1334
CA
ASP
A
216
−3.643
47.933
35.660 
1.00
79.62


ATOM
1335
C
ASP
A
216
−4.311
48.227
36.996
1.00
83.92


ATOM
1336
O
ASP
A
216
−5.489
47.923
37.197
1.00
83.64


ATOM
1337
CB
ASP
A
216
−2.658
46.767
35.814
1.00
81.22


ATOM
1338
CG
ASP
A
216
−1.723
46.631
34.624
1.00
89.59


ATOM
1339
OD1
ASP
A
216
−2.185
46.813
33.477
1.00
90.41


ATOM
1340
OD2
ASP
A
216
−0.529
46.331
34.834
1.00
93.42


ATOM
1341
N
SER
A
217
−3.555
48.835
37.902
1.00
80.61


ATOM
1342
CA
SER
A
217
−4.054
49.154
39.232
1.00
80.60


ATOM
1343
C
SER
A
217
−5.263
50.079
39.222
1.00
85.16


ATOM
1344
O
SER
A
217
−5.768
50.456
40.278
1.00
84.67


ATOM
1345
CB
SER
A
217
−2.941
49.738
40.092
1.00
84.08


ATOM
1346
OG
SER
A
217
−1.748
48.988
39.947 
1.00
92.72


ATOM
1347
N
MET
A
218
−5.733
50.435
38.029
1.00
82.43


ATOM
1348
CA
MET 
A
218
−6.900
51.306
37.899
1.00
82.24


ATOM
1349
CB
MET
A
218
−6.490
52.682
37.369
1.00
84.65


ATOM
1350
C
MET 
A
218
−7.959
50.686
36.993
1.00
85.84


ATOM
1351
O
MET
A
218
−7.636
49.952
36.054
1.00
85.56


ATOM
1352
N
ALA
A
219
−9.223
50.998
37.265
1.00
81.99


ATOM
1353
N
PHE
A
222
−12.863
52.641
39.824
1.00
78.17


ATOM
1354
CA
PHE
A
222
−12.167
53.479
38.849
1.00
77.83


ATOM
1355
C
PHE
A
222
−12.383
52.985
37.415
1.00
80.65


ATOM
1356
O
PHE
A
222
−12.088
51.828
37.096
1.00
80.78


ATOM
1357
CB
PHE
A
222
−10.669
53.542
39.165
1.00
79.64


ATOM
1358
N
VAL
A
223
−12.884
53.871
36.553
1.00
75.60


ATOM
1359
CA
VAL
A
223
−13.133
53.532
35.149
1.00
74.34


ATOM
1360
C
VAL
A
223
−13.039
54.758
34.217
1.00
74.56


ATOM
1361
O
VAL
A
223
−13.694
55.786
34.449
1.00
74.18


ATOM
1362
CB
VAL
A
223
−14.512
52.845
34.963
1.00
78.40


ATOM
1363
CG1
VAL
A
223
−14.342
51.448
34.369
1.00
78.12


ATOM
1364
CG2
VAL
A
223
−15.264
52.783
36.289
1.00
78.16


ATOM
1365
N
GLY
A
224
−12.228
54.632
33.164
1.00
67.59


ATOM
1366
CA
GLY
A
224
−12.031
55.710
32.192
1.00
65.82


ATOM
1367
C
GLY
A
224
−12.807
55.436
30.898
1.00
65.53


ATOM
1368
O
GLY
A
224
−12.827
54.292
30.448
1.00
65.50


ATOM
1369
N
THR
A
225
−13.379
56.485
30.309
1.00
58.19


ATOM
1370
CA
THR
A
225
−14.177
56.344
29.091
1.00
56.05


ATOM
1371
C
THR
A
225
−13.408
55.711
27.923
1.00
54.21


ATOM
1372
O
THR
A
225
−12.255
56.057
27.666
1.00
52.90


ATOM
1373
CB
THR
A
225
−14.798
57.696
28.642
1.00
64.96


ATOM
1374
OG1
THR 
A
225
−15.855
57.459
27.701
1.00
65.16


ATOM
1375
CG2
THR
A
225
−13.744
58.586
27.995
1.00
63.72


ATOM
1376
N
ARG
A
226
−14.064
54.778
27.226
1.00
46.95


ATOM
1377
CA
ARG
A
226
−13.487
54.129
26.043
1.00
44.48


ATOM
1378
C
ARG
A
226
−14.082
54.762
24.790
1.00
42.67


ATOM
1379
O
ARG
A
226
−13.914
54.255
23.684
1.00
40.68


ATOM
1380
CE
ARG
A
226
−13.809
52.629
26.025
1.00
43.80


ATOM
1381
CG
ARG
A
226
−13.915
51.974
27.383
1.00
52.17


ATOM
1332
CD
ARG
A
226
−13.900
50.451
27.233
1.00
54.51


ATOM
1383
NE
ARG
A
226
−12.552
49.941
27.409
1.00
55.72


ATOM
1384
CZ
ARG
A
226
−11.996
48.996
26.670
1.00
62.47


ATOM
1385
NH1
ARG
A
226
−12.682
48.404
25.696
1.00
41.49


ATOM
1386
NH2
ARG
A
226
−10.752
45.627
26.924
1.00
51.10


ATOM
1387
N
SER
A
227
−14.803
55.852
24.979
1.00
37.33


ATOM
1388
CA
SER
A
227
−15.475
56.521
23.871
1.00
36.12


ATOM
1389
C
SER
A
227
−14.547
57.032
22.765
1.00
37.33


ATOM
1390
O
SER
A
227
−15.003
57.279
21.651 
1.00
35.87


ATOM
1391
CB
SER
A
227
−16.419
57.613
24.377
1.00
38.29


ATOM
1392
OG
SER
A
227
−15.707
58.780
24.705
1.00
47.24


ATOM
1393
N
TYR
A
228
−13.234
57.104
23.040 
1.00
32.68


ATOM
1394
CA
TYR
A
228
−12.256
57.534
22.015
1.00
30.97


ATOM
1395
C
TYR
A
228
−11.346
56.396
21.562 
1.00
37.35


ATOM
1396
O
TYR
A
228
−10.398
56.614
20.796 
1.00
37.36


ATOM
1397
CB
TYR
A
228
−11.402
58.716
22.514 
1.00
30.08


ATOM
1398
CG
TYR
A
228
−12.218
59.944
22.844 
1.00
28.57


ATOM
1399
CD1
TYR
A
228
−12.509
60.895
21.869 
1.00
28.54


ATOM
1400
CD2
TYR
A
228
−12.728
60.133
24.119 
1.00
29.30


ATOM
1401
CE1
TYR
A
228
−13.297
61.995
22.153 
1.00
27.01


ATOM
1402
CE2
TYR
A
228
−13.512
61.237
24.421 
1.00
30.10


ATOM
1403
CZ
TYR
A
228
−13.785
62.169
23.432 
1.00
32.95


ATOM
1404
OH
TYR
A
228
−14.535
63.271
23.736
1.00
29.42


ATOM
1405
N
MET
A
229
−11.640
55.180
22.017
1.00
34.82


ATOM
1406
CA
MET
A
229
−10.835
54.013
21.653
1.00
35.21


ATOM
1407
C
MET
A
229
−11.057
53.584
20.205 
1.00
37.74


ATOM
1408
O
MET
A
229
−12.170
53.633
19.701
1.00
36.90


ATOM
1409
CB 
MET
A
229
−11.139
52.850
22.588
1.00
38.44


ATOM
1410
CG 
MET
A
229
−10.603
53.054
23.981
1.00
43.70


ATOM
1411
SD 
MET
A
229
−10.428
51.509
24.871
1.00
49.14


ATOM
1412
CE 
MET
A
229
−9.909
52.154
26.498 
1.00
45.88


ATOM
1413
N
SER
A
230
−9.993
53.160
19.539 
1.00
34.37


ATOM
1414
CA
SER
A
230
−10.114
52.719
18.152
1.00
35.11


ATOM
1415
C
SER
A
230
−10.927
51.428
18.091
1.00
39.92


ATOM
1416
O
SER
A
230
−11.006
50.691
19.072
1.00
39.60


ATOM
1417
CB
SER
A
230
−8.729
52.499
17.530
1.00
38.83


ATOM
1418
OG
SER
A
230
−7.995
51.512
18.246
1.00
48.18


ATOM
1419
N
PRO
A
231
−11.505
51.141
16.929
1.00
36.80


ATOM
1420
CA
PRO
A
231
−12.276
49.901
16.745
1.00
35.85


ATOM
1421
C
PRO
A
231
−11.422
48.651
17.052
1.00
39.50


ATOM
1422
O
PRO
A
231
−11.885
47.727
17.696
1.00
36.98


ATOM
1423
CB
PRO
A
231
−12.650
49.932
15.247
1.00
37.27


ATOM
1424
CG
PRO
A
231
−12.341
51.346
14.780
1.00
41.37


ATOM
1425
CD
PRO
A
231
−11.236
51.822
15.651
1.00
36.83


ATOM
1426
N
GLU
A
232
−10.172
48.648
16.604
1.00
37.24


ATOM
1427
CA
GLU
A
232
−9.291
47.511
16.838
1.00
37.76


ATOM
1428
C
GLU
A
232
−9.043
47.271
18.327
1.00
45.46


ATOM
1429
O
GLU
A
232
−8.968
46.123
18.767
1.00
44.87


ATOM
1430
CB
GLU
A
232
−7.967
47.640
16.053
1.00
38.53


ATOM
1431
CG
GLU
A
232
−6.957
48.640
16.639
1.00
44.10


ATOM
1432
CD
GLU
A
232
−6.985
50.001
15.937
1.00
51.28


ATOM
1433
OE1
GLU
A
232
−8.009
50.332
15.318
1.00
29.96


ATOM
1434
OE2
GLU
A
232
−5.980
50.735
16.007
1.00
44.19


ATOM
1435
N
ARG
A
233
−8.949
48.358
19.102
1.00
43.38


ATOM
1436
CA
ARG 
A
233
−8.749
48.257
20.552
1.00
43.35


ATOM
1437
C
ARG
A
233
−10.021
47.800
21.247
1.00
47.40


ATOM
1438
O
ARG
A
233
−9.974
47.072
22.243
1.00
46.20


ATOM
1439
CB
ARG
A
233
−8.322
49.601
21.137
1.00
42.86


ATOM
1440
CG
ARG
A
233
−6.823
49.771
21.205
1.00
50.67


ATOM
1441
CD
ARG
A
233
−6.440
50.890
22.160
1.00
57.63


ATOM
1442
NE
ARG
A
233
−6.588
50.493
23.558
1.00
59.57


ATOM
1443
CZ
ARG
A
233
−6.216
51.286
24.585
1.00
69.16


ATOM
1444
NH1
ARG
A
233
−5.886
52.525
24.369
1.00
52.85


ATOM
1445
NH2
ARG
A
233
−6.467
50.842
25.826
1.00
52.70


ATOM
1446
N
LEU
A
234
−11.160
48.256
20.737
1.00
44.85


ATOM
1447
CA
LEU
A
234
−12.447
47.880
21.300
1.00
45.64


ATOM
1448
C
LEU
A
234
−12.785
46.419
20.915
1.00
52.91


ATOM
1449
O
LEU
A
234
−13.633
45.779
21.535
1.00
52.33


ATOM
1450
CB
LEU
A
234
−13.542
48.826
20.782
1.00
45.43


ATOM
1451
CG
LEU
A 
234
−13.533
50.266
21.305
1.00
49.54


ATOM
1452
CD1
LEU
A
234
−14.682
51.051
20.711
1.00
49.16


ATOM
1453
CD2
LEU
A
234
−13.602
50.287
22.834
1.00
52.87


ATOM
1454
N
GLN
A
235
−12.114
45.512
19.888
1.00
51.72


ATOM
1455
CA
GLN
A
235
−12.374
44.565
19.398
1.00
52.72


ATOM
1456
C
GLN
A
235
−11.426
43.516
19.982
1.00
60.13


ATOM
1457
O
GLN
A
235
−11.466
42.356
19.597
1.00
59.38


ATOM
1458
CB
GLN
A
235
−12.324
44.539
17.868
1.00
53.75


ATOM
1459
CG
GLN
A 
235
−13.687
44.555
17.197
1.00
69.87


ATOM
1460
CD
GLN
A
235
−13.634
44.069
15.754
1.00
95.11


ATOM
1461
OE1
GLN
A
235
−12.564
44.017
15.140
1.00
91.03


ATOM
1462
NE2
GLN
A
235
−14.796
43.719
15.203
1.00
88.72


ATOM
1463
N
GLY
A
236
−10.574
43.936
20.910
1.00
59.96


ATOM
1464
CA
GLY
A
236
−9.639
43.019
21.555
1.00
61.15


ATOM
1465
C
GLY
A
236
−8.354
42.834
20.751
1.00
68.92


ATOM
1466
O
GLY
A
236
−7.333
42.403
21.290
1.00
69.16


ATOM
1467
N
THR
A
237
−8.407
43.144
19.463
1.00
67.94


ATOM
1468
CA
THR
A
237
−7.228
43.032
18.616
1.00
68.89


ATOM
1469
C
THR
A
237
−6.137
43.936
19.183
1.00
75.83


ATOM
1470
O
THR
A
237
−6.351
45.144
19.344
1.00
75.75


ATOM
1471
CB
THR
A
237
−7.532
43.460
17.178
1.00
77.60


ATOM
1472
OG1
THR
A
237
−8.237
42.411
16.506
1.00
78.51


ATOM
1473
CG2
THR
A
237
−6.245
43.766
16.426
1.00
76.85


ATOM
1474
N
HIS
A
238
−4.986
43.352
19.521
1.00
73.93


ATOM
1475
CA
HIS
A
238
−3.887
44.130
20.097
1.00
74.36


ATOM
1476
C
HIS
A
229
−3.575
45.370
19.264
1.00
76.04


ATOM
1477
O
HIS
A
238
−3.492
45.311
18.031
1.00
75.72


ATOM
1478
CB
HIS
A
238
−2.625
43.268
20.333
1.00
75.91


ATOM
1479
CG
HIS
A
238
−1.960
43.530
21.651
1.00
80.14


ATOM
1480
ND1
HIS
A
238
−2.670
43.704
22.822
1.00
82.36


ATOM
1481
CD2
HIS
A
238
−0.654
43.689
21.978
1.00
82.54


ATOM
1482
CE1
HIS
A
238
−1.829
43.940
23.815
1.00
82.09


ATOM
1483
NE2
HIS
A
238
−0.599
43.935
23.330
1.00
82.40


ATOM
1484
N
TYR
A
239
−3.460
46.503
19.944
1.00
70.51


ATOM
1485
CA
TYR
A
239
−3.259
47.777
19.276
1.00
69.01


ATOM
1486
C
TYR
A
239
−1.816
48.266
19.257
1.00
67.50


ATOM
1487
O
TYR
A
239
−0.927
47.662
19.853
1.00
66.93


ATOM
1488
CB
TYR
A
239
−4.144
48.832
19.928
1.00
70.69


ATOM
1489
CG
TYR
A
239
−3.972
48.932
21.432
1.00
73.42


ATOM
1490
CD1
TYR
A
239
−4.546
47.991
22.284
1.00
75.70


ATOM
1491
CD2
TYR
A
239
−3.275
49.992
22.001
1.00
74.16


ATOM
1492
CE1
TYR
A
239
−4.409
48.096
23.659
1.00
76.81


ATOM
1493
CE2
TYR
A
239
−3.129
50.100
23.367
1.00
75.10


ATOM
1494
CZ
TYR
A
239
−3.692
49.153
24.193
1.00
82.68


ATOM
1495
OH
TYR
A
239
−3.538
49.271
25.553
1.00
83.99


ATOM
1496
N
SER
A
240
−1.611
49.395
18.587
1.00
59.79


ATOM
1497
CA
SER 
A
240
−0.307
50.035
18.518
1.00
57.27


ATOM
1498
C
SER
A
240
−0.505
51.546
18.566
1.00
55.43


ATOM
1499
O
SER 
A
240
−1.543
52.027
19.012
1.00
54.14


ATOM
1500
CB
SER
A
240.
0.415
49.642
17.233
1.00
59.80


ATOM
1501
OG
SER
A
240
0.005
50.456
16.155
1.00
65.92


ATOM
1502
N
VAL
A
241
0.485
52.288
18.087
1.00
49.05


ATOM
1503
CA
VAL
A
241
0.385
53.736
18.048
1.00
47.75


ATOM
1504
C
VAL
A
241
−0.740
54.145
17.106
1.00
47.36


ATOM
1505
O
VAL
A
241
−1.328 
55.217
17.257
1.00
46.67


ATOM
1506
CB
VAL
A
241
1.705 
54.387
17.595
1.00
52.45


ATOM
1507
CG1
VAL
A
241
1.684
55.909
17.889
1.00
52.31


ATOM
1508
CH2
VAL
A
241
2.897
53.714
18.303
1.00
52.56


ATOM
1509
N
GLN
A
242
−1.052
53.271
16.149
1.00
40.50


ATOM
1510
CA
GLN
A
242
−2.118 
53.539
15.194
1.00
38.87


ATOM
1511
C
GLN
A
242
−3.403 
53.901
15.938
1.00
40.18


ATOM
1512
O
GLN
A
242
−4.141 
54.775
15.514
1.00
39.96


ATOM
1513
CB
GLN
A
242
−2.356
52.321
14.287
1.00
39.85


ATOM
1514
CG
GLN
A
242
−1.248
52.065
13.274
1.00
45.36


ATOM
1515
CD
GLN
A
242
−0.879 
53.307
12.469
1.00
59.35


ATOM
1516
OE1
GLN
A
242
0.027 
54.053
12.838
1.00
51.36


ATOM
1517
NE2
GLN 
A
242
−1.543 
53.495
11.329
1.00
49.91


ATOM
1518
N
SER 
A
243
−3.654
53.219
17.052
1.00
34.99


ATOM
1519
CA
SER
A
243
−4.835 
53.475
17.867
1.00
33.85


ATOM
1520
C
SER
A
243
−4.884 
54.901
18.456
1.00
36.12


ATOM
1521
O
SER
A
243
−5.962 
55.438
18.698
1.00
35.52


ATOM
1522
CB
SER
A
243
−4.945 
52.438
18.963
1.00
37.92


ATOM
1523
OG
SER
A
243
−4.323 
51.246
18.546
1.00
51.67


ATOM
1524
N
ASP
A
244
−3.715 
55.504
18.669
1.00
31.88


ATOM
1525
CA
ASP
A
244
−3.626 
56.877
19.187
1.00
30.94


ATOM
1526
C
ASP
A
244
−4.009 
57.867
18.070
1.00
34.54


ATOM
1527
O
ASP
A
244
−4.624
58.906
18.309
1.00
33.66


ATOM
1528
CB
ASP
A
244
−2.197 
57.162
19.674
1.00
31.88


ATOM
1529
CG
ASP 
A
244
−1.895
56.512
21.016
1.00
36.68


ATOM
1530
OD1
ASP
A
244
−2.849
56.143
21.745
1.00
35.28


ATOM
1531
OD2
ASP
A
244
−0.708
56.382
21.350
1.00
41.96


ATOM
1532
N
ILE
A
245
−3.666
57.510
16.842
1.00
31.35


ATOM
1533
CA
ILE
A
245
−3.976
58.340
15.688
1.00
30.40


ATOM
1534
C
ILE
A
245
−5.483
58.407
15.452
1.00
32.16


ATOM
1535
O
ILE
A
245
−6.035 
59.463
15.110
1.00
31.42


ATOM
1536
CB
ILE
A
245
−3.222
57.849
14.449
1.00
33.34


ATOM
1537
CG1
ILE
A
245
−1.738
58.314
14.544
1.00
33.05


ATOM
1538
CG2
ILE
A
245
−3.932
58.324
13.121
1.00
33.28


ATOM
1539
CD1
ILE
A
245
−0.801
57.603
13.595
1.00
33.32


ATOM
1540
N
TRP
A
246
−6.158
57.301
15.714
1.00
28.46


ATOM
1541
CA
TRP
A
246
−7.603
57.256
15.572
1.00
28.53


ATOM
1542
C
TRP
A
246
−8.208
58.220
16.602
1.00
32.05


ATOM
1543
O
TRP
A
246
−9.080
59.032
16.280
1.00
31.70


ATOM
1544
CB
TRP
A
246
−8.128
55.827
15.829
1.00
27.72


ATOM
1545
CG
TRP
A
246
−9.574
55.796
16.232
1.00
29.11


ATOM
1546
CD1
TRP
A
246
−10.095
56.086
17.471 
1.00
32.27


ATOM
1547
CD2
TSP
A
246
−10.693
55.599
15.368 
1.00
29.44


ATOM
1548
NE1
TRP
A
246
−11.467 
36.038
17.431
1.00
31.92


ATOM
1549
CE2
TRP
A
246
−11.861 
55.728
16.155 
1.00
33.49


ATOM
1550
CE3
TRP
A
246
−10.826
55.258
14.015
1.00
30.85


ATOM
1551
CZ2
TRP
A
246
−13.135 
55.569
15.629 
1.00
32.92


ATOM
1552
CZ3
TRP
A
246
−12.102 
55.107
13.494 
1.00
32.55


ATOM
1553
CH2
TRP
A
246
−13.236
55.288
14.291 
1.00
33.24


ATOM
1554
N
SER
A
247
−7.763 
58.085
17.852
1.00
28.17


ATOM
1555
CA
SER
A
247
−8.271
58.910
18.955
1.00
27.59


ATOM
1556
C
SER
A
247
−8.065 
60.381
18.661
1.00
30.51


ATOM
1557
O
SER
A
247
−8.915
61.215
18.991
1.00
30.51


ATOM
1558
CB
SER
A
247
−7.578
58.525
20.269
1.00
29.89


ATOM
1559
OG
SER
A
247
−7.830
57.158
20.536
1.00
35.32


ATOM
1560
N
MET
A
248
−6.936
60.700
18.040
1.00
26.41


ATOM
1561
CA
MET
A
248
−6.652
62.067
17.671.
1.00
25.98


ATOM
1562
C
MET
A
248
−7.641
62.495
16.621
1.00
29.06


ATOM
1563
O
MET
A
248
−8.221
63.563
16.712
1.00
29.04


ATOM
1564
CB
MET
A
248
−5.230
62.225
17.122
1.00
27.89


ATOM
1565
CG
MET
A
248
−4.929
63.665
16.657
1.00
30.64


ATOM
1566
SD
MET
A
248
−3.339
63.842
15.852
1.00
34.02


ATOM
1567
CE
MET
A
248
−3.631
62.889
14.317
1.00
30.31


ATOM
1568
N
GLY
A
249
−7.826
61.655
15.606
1.00
25.78


ATOM
1569
CA
GLY
A
249
−8.757
61.973
14.521
1.00
25.42


ATOM
1570
C
GLY
A
249
−10.150
62.268
15.070
1.00
29.91


ATOM
1571
O
GLY
A
249
−10.793
63.246
14.681
1.00
30.39


ATOM
1572
N
LEU
A
250
−10.602
61.420
15.981
1.00
26.99


ATOM
1573
CA
LEU
A
250
−11.933
61.549
16.585
1.00
27.07


ATOM
1574
C
LEU
A
250
−12.033
62.815
17.442
1.00
29.50


ATOM
1575
O
LEU
A
250
−13.004
63.552
17.361
1.00
27.76


ATOM
1576
CB
LEU
A
250
−12.261
60.292
17.421
1.00
27.00


ATOM
1577
CG
LEU
A
250
−13.670
60.258
18.037
1.00
32.57


ATOM
1578
CD1
LEU
A
250
−14.707
60.568
16.973
1.00
33.97


ATOM
1579
CD2
LEU
A
250
−13.966
58.942
18.716
1.00
33.08


ATOM
1580
N
SER
A
251
−11.006
63.065
18.244
1.00
27.23


ATOM
1581
CA
SER
A
251
−10.952
64.284
19.078
1.00
26.54


ATOM
1582
C
SER
A
251
−10.960
65.534
18.192
1.00
29.01


ATOM
1583
O
SER
A
251
−11.556
66.554
18.550
1.00
27.52


ATOM
1584
CB
SER
A
251
−9.698
64.272
19.972
1.00
27.98


ATOM
1585
OG
SER
A
251
−9.671
63.087
20.759
1.00
32.73


ATOM
1586
N
LEU
A
252
−10.312
65.450
17.027
1.00
26.00


ATOM
1587
CA
LEU
A
252
−10.292
65.589
16.109
1.00
26.53


ATOM
1588
C
LEU
A
252
−11.683
66.903
15.537
1.00
30.23


ATOM
1589
O
LEU
A
252
−12.065
68.068
15.414
1.00
29.42


ATOM
1590
CB
LEU
A
252
−9.283
66.384
14.963
1.00
26.52


ATOM
1591
CG
LEU
A
252
−7.803
66.507
15.338
1.00
30.98


ATOM
1592
CD1
LEU
A
252
−6.892
66.046
14.172
1.00
30.25


ATOM
1593
CD2
LEU
A
252
−7.466
67.950
15.790
1.00
31.66


ATOM
1594
N
VAL
A
253
−12.423
65.872
15.152
1.00
27.03


ATOM
1595
CA
VAL
A
253
−13.766
66.101
14.587
1.00
26.19


ATOM
1596
C
VAL
A
253
−14.699
66.643
15.650
1.00
30.13


ATOM
1597
O
VAL
A
253
−15.451
67.578
15.403
1.00
31.28


ATOM
1598
CB
VAL
A
253
−14.353
64.831
13.959
1.00
29.46


ATOM
1599
CG1
VAL
A
253
−15.819
65.089
13.457
1.00
29.05


ATOM
1600
CG2
VAL
A
253
−13.462
64.346
12.825
1.00
28.45


ATOM
1601
N
GLU
A
254
−14.596
66.114
16.863
1.00
26.03


ATOM
1602
CA
GLU
A
254
−15.421
66.611
17.941
1.00
25.78


ATOM
1603
C
GLU
A
254
−15.183
68.104
18.153
1.00
31.56


ATOM
1604
O
GLU
A
254
−16.131
68.885
18.355
1.00
32.14


ATOM
1605
CB
GLU
A
254
−15.125
65.888
19.234
1.00
26.92


ATOM
1606
CG
GLU
A
254
−15.704
66.624
20.459
1.00
29.75


ATOM
1607
CD
GLU
A
254
−15.620
65.820
21.725
1.00
36.66


ATOM
1608
OE1
GLU
A
254
−15.090
64.700
21.686
1.00
36.73


ATOM
1609
OE2
GLU
A
254
−16.096
66.301
22.765
1.00
29.17


ATOM
1610
N
MET
A
255
−13.910
68.487
18.175
1.00
27.63


ATOM
1611
CA
MET
A
255
−13.518
69.874
18.395
1.00
27.41


ATOM
1612
C
MET
A
255
−13.949
70.793
17.246
1.00
29.26


ATOM
1613
O
MET
A
255
−14.322
71.938
17.473
1.00
27.94


ATOM
1614
CB
MET
A
255
−12.009
69.961
18.628
1.00
29.69


ATOM
1615
CG
MET
A
255
−11.576
69.397
19.994
1.00
33.36


ATOM
1616
SD
MET
A
255
−9.852
69.651
20.354
1.00
37.59


ATOM
1617
CE
MET
A
255
−9.111
68.408
19.265
1.00
33.60


ATOM
1618
N
ALA
A
256
−13.897
70.276
16.020
1.00
25.00


ATOM
1619
CA
ALA
A
256
−14.291
71.043
14.835
1.00
25.44


ATOM
1620
C
ALA
A
256
−15.820
71.212 
14.743
1.00
30.83


ATOM
1621
O
ALA
A
256
−16.245
72.260
14.273
1.00
29.78


ATOM
1622
CB
ALA
A
256
−13.802
70.329
13.550
1.00
25.63


ATOM
1623
N
VAL
A
257
−16.620
70.325
15.124
1.00
29.53


ATOM
1624
CA
VAL
A
257
−18.06.8 
70.444
15.007
1.00
30.69


ATOM
1625
C
VAL
A
257
−18.766
70.850
16.294
1.00
35.95


ATOM
1626
O
VAL
A
257
−19.939
71.222
16.279
1.00
35.13


ATOM
1627
CB
VAL
A
257
−18.705
69.169
14.411
1.00
34.67


ATOM
1628
CG1
VAL
A
257
−17.972
68.769
13.127
1.00
34.21


ATOM
1629
CG2
VAL
A
257
−18.668
68.045
15.407
1.00
34.38


ATOM
1630
N
GLY
A
258
−18.025
70.801
17.405
1.00
33.58


ATOM
1631
CA
GLY
A
258
−18.563
71.251
18.688
1.00
33.74


ATOM
1632
C
GLY
A
258
−19.330
70.199
19.476
1.00
38.14


ATOM
1633
O
GLY
A
258
−20.055
70.526
20.405
1.00
36.93


ATOM
1634
N
ARG
A
259
−19.141
68.936
19.135
1.00
36.15


ATOM
1635
CA
ARG
A
259
−19.812
67.878
19.869
1.00
36.18


ATOM
1636
C
ARG
A
259
−19.217
66.525
19.542
1.00
38.38


ATOM
1637
O
ARG
A
259
−18.666
66.329
18.457
1.00
36.60


ATOM
1638
CB
ARG
A
259
−21.315
67.895
19.554
1.00
38.19


ATOM
1629
CG
ARG
A
259
−21.924
66.531
19.383
1.00
49.32


ATOM
1640
CD
ARG
A
259.
−23.076
66.562
18.415
1.00
62.68


ATOM
1641
NE
ARG
A
259
−22.901
65.572
17.359
1.00
74.91


ATOM
1642
CZ
ARG
A
259.
−23.803
64.659
17.035
1.00
85.18


ATOM
1643
NH1
ARG
A
259.
−24.960
64.620
17.667
1.00
69.94


ATOM
1644
NR2
ARG
A
259
−23.552
63.796
16.068
1.00
76.65


ATOM
1645
N
TYR
A
260
−19.307
65.592
20.490
1.00
35.77


ATOM
1646
CA
TYR
A
260
−18.822
64.237
20.249
1.00
35.90


ATOM
1647
C
TYR
A
260.
−19.586
63.750
19.013
1.00
40.56


ATOM
1648
O
TYR
A
260
−20.813
63.763
18.993
1.00
39.41


ATOM
1649
CB
TYR
A
260
−19.094
63.348
21.458
1.00
36.83


ATOM
1650
CG
TYR
A
260
−18.638
61.913
21.285
1.00
38.79


ATOM
1651
CD1
TYR
A
260
−17.290 
61.574
21.346
1.00
39.93


ATOM
1652
CD2
TYR
A
260
−19.560
60.896
21.051
1.00
29.66


ATOM
1653
CE1
TYR
A
260
−16.879
60.261
21.190
1.00
38.61


ATOM
1654
CE2
TYR
A
260
−19.152
59.588
20.885
1.00
40.44


ATOM
1655
CZ
TYR
A
260
−17.809
59.276
20.977
1.00
44.25


ATOM
1656
OH
TYR
A
260
−17.410
57.961
20.840
1.00
41.29


ATOM
1657
N
PRO
A
261
−18.840
63.408
17.964
1.00
39.07


ATOM
1658
CA
PRO
A
261
−19.399
63.102
16.651
1.00
38.60


ATOM
1659
C
PRO
A
261
−20.077
61.752
16.365
1.00
44.14


ATOM
1660
O
PRO
A
261
−20.385
61.455
15.217
1.00
44.61


ATOM
1661
CB
PRO
A
261
−18.206
63.304
15.726
1.00
39.80


ATOM
1662
CG
PRO
A
261
−17.021
62.915
16.561
1.00
44.28


ATOM
1663
CD
PRO
A
261
−17.386
63.156
18.014
1.00
39.82


ATOM
1664
N
ILE
A
262
−20.306
60.942 
17.383
1.00
41.56


ATOM
1665
CA
ILE
A
262
−20.987
59.654
17.190
1.00
41.57


ATOM
1666
C
ILE
A
262
−22.195
59.578
18.110
1.00
45.98


ATOM
1667
O
ILE
A
262
−22.070
59.753
19.314
1.00
45.22


ATOM
1668
CB
ILE
A
262
−20.070
58.453 
17.518
1.00
44.60


ATOM
1669
CG1
ILE
A
262
−18.826
58.467
16.648
1.00
44.38


ATOM
1670
CG2
ILE
A
262
−20.819
57.146
17.312
1.00
45.37


ATOM
1671
CD1
ILE
A
262
−17.772
57.508
17.110
1.00
46.80


ATOM
1672
N
PRO
A
263
−23.370
59.326
17.535
1.00
43.93


ATOM
1673
CA
PRO
A
263
−23.499
59.119
16.103
1.00
43.68


ATOM
1674
C
PRO
A
263
−23.433
60.454 
15.266
1.00
48.14


ATOM
1675
O
PRO
A
263
−23.609
61.505
15.962
1.00
46.93


ATOM
1676
CB
PRO
A
263
−24.891
58.509
15.977
1.00
45.35


ATOM
1677
CG
PRO
A
263
−25.683
59.147
17.109
1.00
49.50


ATOM
1678
CD
PRO
A
263
−24.671
59.621
18.161
1.00
44.77


ATOM
1679
N
PRO
A
264
−23.173
60.400
14.066
1.00
46.61


ATOM
1680
CA
PRO
A
264
−23.042
61.612
13.252
1.00
46.86


ATOM
1681
C
PRO
A
254
−24.264
52.538
13.279
1.00
53.95


ATOM
1682
O
PRO
A
264
−25.401
62.083
13.399
1.00
53.34


ATOM
1683
CB
PRO
A
264
−22.819
61.061
11.838
1.00
47.89


ATOM
1684
CG
PRO
A
264
−23.286
59.700
11.864
1.00
51.83


ATOM
1685
CD
PRO
A
264
−23.177
59.178
13.245
1.00
47.08


ATOM
1686
N
PRO
A
265
−24.010
63.838
13.160
1.00
52.74


ATOM
1687
CA
PRO
A
265
−25.073
64.850
13.132
1.00
53.09


ATOM
1688
C
PRO
A
265
−25.841
64.772
11.806
1.00
60.33


ATOM
1689
O
PRO
A
265
−25.285
64.400
10.777
1.00
59.31


ATOM
1690
CB
PRO
A
265
−24.302
66.1.79 
13.191
1.00
54.28


ATOM
1691
CG
PRO
A
265
−22.954
65.830
13.751
1.00
58.50


ATOM
1692
CD
PRO
A
265
−22.669
64.436
13.283
1.00
53.59


ATOM
1693
N
ASP
A
266
−27.117
65.144
11.841
1.00
60.41


ATOM
1694
CA
ASP
A
266
−27.963
65.110
10.651 
1.00
61.49


ATOM
1695
C
ASP
A
266
−27.787
66.366
9.821
1.00
66.58


ATOM
1696
O
ASP
A
266
−27.154
67.330
10.261
1.00
66.08


ATOM
1697
CB
ASP
A
266
−29.436
64.970
11.048
1.00
63.72


ATOM
1698
CG
ASP 
A
266
−29.690
63.751
11.907
1.00
78.58


ATOM
1699
OD1
ASP 
A
266
−28.795
62.873
11.976
1.00
79.20


ATOM
1700
OD2
ASP
A
266
−30.776
63.676
12.525
1.00
86.02


ATOM
1701
N
ALA
A
267
−28.366
66.363
8.625
1.00
63.90


ATOM
1702
CA
ALA
A
267
−28.304
67.534
7.766
1.00
63.92


ATOM
1703
C
ALA
A
267
−28.931
68.691
8.533
1.00
67.67


ATOM
1704
O
ALA
A
267
−28.522
69.840
8.393
1.00
67.07


ATOM
1705
CB
ALA
A
267
−29.063
67.278
6.464
1.00
64.69


ATOM
1706
N
LYS
A
268
−29.900
68.355
9.384
1.00
64.48


ATOM
1707
CA
LYS
A
268
−30.604
69.333
10.198
1.00
64.15


ATOM
1708
C
LYS
A
268
−29.739
69.885
11.319
1.00
67.40


ATOM
1709
O
LYS
A
268
−29.734
71.092
11.570
1.00
67.40


ATOM
1710
CB
LYS
A
268
−31.880
68.725
10.770
1.00
67.32


ATOM
1711
CG
LYS
A
268
−31.718
68.102
12.152
1.00
84.28


ATOM
1712
CD
LYS
A
268
−32.990
67.365
12.573
1.00
94.08


ATOM
1713
CE
LYS
A
268
−34.172
66.322
12.700
1.00
103.24


ATOM
1714
NZ
LYS
A
268
−35.413
67.771
12.083
1.00
111.76


ATOM
1715
N
GLU
A
269
−29.019
69.003
12.009
1.00
62.84


ATOM
1716
CA
GLU
A
269
−28.131
69.437
13.088
1.00
61.93


ATOM
1717
C
GLU
A
269
−26.991
70.251
12.479
1.00
63.49


ATOM
1718
O
GLU
A
269
−26.614
71.306
12.993
1.00
62.30


ATOM
1719
CB
GLU
A
269
−27.569
68.231
13.843
1.00
63.48


ATOM
1720
CG
GLU
A
269
−28.626
67.262
14.358
1.00
74.79


ATOM
1721
CD
GLU
A
269
−28.021
65.961
14.861
1.00
92.79


ATOM
1722
OE1
GLU
A
269
−27.204
66.017
15.808
1.00
88.58


ATOM
1723
OE2
GLU
A
269
−28.334
64.891
14.287
1.00
77.62


ATOM
1724
N
LEU
A
270
−26.471
69.758
11.361
1.00
58.98


ATOM
1725
CA
LEU
A
270
−25.404
70.428
10.638
1.00
58.49


ATOM
1726
C
LEU
A
270
−25.863
71.815
10.186
1.00
62.27


ATOM
1727
O
LEU
A
270
−25.095
72.782
10.223
1.00
61.09


ATOM
1728
CB
LEU
A
270
−24.986
69.589
9.435
1.00
58.44


ATOM
1729
CG
LEU
A
270
−24.163
68.353
9.793
1.00
62.55


ATOM
1730
CD1
LEU
A
270
−23.951
67.478
8.558
1.00
62.54


ATOM
1731
CD2
LEU
A
270
−22.836
68.778
10.401
1.00
64.10


ATOM
1732
N
GLU
A
271
−27.128
71.905
9.785
1.00
59.44


ATOM
1733
CA
GLU
A
271
−27.717
73.173
9.366
1.00
59.49


ATOM
1734
C
GLU
A
271
−27.735
74.136
10.556
1.00
62.32


ATOM
1735
O
GLU
A
271
−27.354
75.293
10.439
1.00
62.12


ATOM
1736
CB
GLU 
A
271
−29.146
72.954
8.844
1.00
60.96


ATOM
1737
CG
GLU
A
271
−29.992 
74.226
8.769
1.00
73.96


ATOM
1738
CD
GLU
A
271
−31.472
73.950
9.001
1.00
101.22


ATOM
1739
OE1
GLU
A
271
−32.099
73.290
8.150
1.00
98.41


ATOM
1740
OE2
GLU
A
271
−32.006
74.410
10.039
1.00
98.47


ATOM
1741
N
LEU
A
272
−28.160
73.637
11.703
1.00
58.03


ATOM
1742
CA
LEU
A
272
−28.199
74.447
12.907
1.00
57.77


ATOM
1743
C
LEU
A
272
−26.779
74.818
13.331 
1.00
59.99


ATOM
1744
O
LEU
A
272
−26.511
75.960
13.706
1.00
59.33


ATOM
1745
CB
LEU
A
272
−28.891
73.679
14.035
1.00
58.10


ATOM
1746
CG
LEU
A
272
−30.163
72.928
13.634 
1.00
63.45


ATOM
1747
CD1
LEU
A
272
−30.641
72.0.07
14.762
1.00
63.53


ATOM
1748
CD2
LEU
A
272
−31.266
73.915
13.220
1.00
66.21


ATOM
1749
N
MET
A
273
−25.875
73.837
13.261
1.00
55.25


ATOM
1750
CA
MET
A
273
−24.476
74.019
13.651
1.00
53.69


ATOM
1751
C
MET
A
273
−23.723
75.038
12.787 
1.00
55.73


ATOM
1752
O
MET
A
273
−23.147
75.987
13.307 
1.00
55.38


ATOM
1753
CB
MET
A
273
−23.736
72.677
13.632 
1.00
55.85


ATOM
1754
CG
MET
A
273
−24.264
71.650
14.623
1.00
59.42


ATOM
1755
SD
MET
A
273
−23.500
70.011
14.427
1.00
63.42


ATOM
1756
CE
MET
A
273
−22.468
69.922
15.906
1.00
59.92


ATOM
1757
N
PHE
A
274
−23.713
74.827
11.472
1.00
50.90


ATOM
1758
CA
PHE
A
274
−22.971
75.713
10.576
1.00
50.32


ATOM
1759
C
PHE
A
274
−23.824
76.546
9.627
1.00
57.45


ATOM
1760
O
PHE
A
274
−23.288
77.347
8.843
1.00
56.78


ATOM
1761
CB
PHE
A 
274
−21.950
74.919
9.761
1.00
51.11


ATOM
1762
CG
PHE
A
274
−20.992
74.132
10.592
1.00
51.46


ATOM
1763
CD1
PHE
A
274
−21.342
72.885
11.086
1.00
54.02


ATOM
1764
CD2
PHE
A 
274
−19.725
74.622
10.859
1.00
52.22


ATOM
1765
CE1
PHE
A 
274
−20.450
72.152
11.845
1.00
54.29


ATOM
1766
CE2
PHE
A 
274
−18.828
73.888
11.602 
1.00
54.59


ATOM
1767
CZ
PHE
A
274
−19.187
72.656
12.096 
1.00
52.63


ATOM
1768
N
GLY
A
275
−25.142
76.342
9.659
1.00
55.99


ATOM
1769
CA
GLY
A
275
−26.047
77.080
8.769
1.00
56.10


ATOM
1770
C
GLY
A
275
−25.828
76.677
7.311
1.00
60.59


ATOM
1771
O
GLY
A
275
−26.018
77.486
6.405
1.00
61.02


ATOM
1772
N
GYS
A
276
−25.293
75.475
7.104
1.00
56.87


ATOM
1773
N
PRO
A
306
−30.043
59.289
23.161
1.00
66.36


ATOM
1774
CA
PRO
A
306
−29.058
59.326
24.238 
1.00
65.46


ATOM
1775
C
PRO
A
306
−28.332
57.989
24.345 
1.00
68.29


ATOM
1776
O
PRO
A
306
−28.357
57.343
25.394
1.00
68.58


ATOM
1777
CB
PRO
A
306
−29.916
59.550
25.484
1.00
67.13


ATOM
1778
CG
PRO
A
306
−31.140
60.213
24.983
1.00
71.71


ATOM
1779
CD
PRO
A
306
−31.396
59.607
23.644
1.00
67.06


ATOM
1780
N
MET
A
307
−27.694
57.583
23.247
1.00
62.75


ATOM
1781
CA
MET
A
307
−26.963
56.314
23.160
1.00
61.62


ATOM
1782
C
MET
A
307
−26.172
55.925
24.415
1.00
63.02


ATOM
1783
O
MET
A
307
−25.235
56.618
24.810
1.00
62.32


ATOM
1784
CB
MET
A
307
−26.016
56.345
21.960
1.00
63.94


ATOM
1785
CG
MET
A
307
−26.242
55.246
20.952
1.00
67.38


ATOM
1786
SD
MET
A 
307
−25.201
53.451
19.491
1.00
71.36


ATOM
1787
CE
MET
A 
307
−24.735
53.790
19.187
1.00
67.99


ATOM
1788
N
ALA
A 
308
−26.528
54.786 
25.007
1.00
57.80


ATOM
1769
CA
ALA
A
308
−25.798
54.272
26.162
1.00
56.71


ATOM
1790
C
ALA
A 
308
−24.398
53.876
25.694
1.00
58.37


ATOM
1791
O
ALA
A 
308
−24.201
53.548
24.523 
1.00
57.57


ATOM
1792
CB
ALA
A 
308
−26.522
53.072
26.756
1.00
57.42


ATOM
1793
N
ILE
A 
309
−23.426
53.935
26.601
1.00
53.88


ATOM
1794
CA
ILE
A
309
−22.036
53.631 
26.265
1.00
52.75


ATOM
1795
C
ILE
A 
309
−21.855
52.334 
25.469
1.00
52.93


ATOM
1796
O
ILE
A 
309
−21.141
52.315
24.464
1.00
52.33


ATOM
1797
CB
ILE
A 
309
−21.115
53.631
27.517
1.00
56.34


ATOM
1798
CG1
ILE
A 
309
−20.528
55.023
27.743
1.00
57.29


ATOM
1799
CG2
ILE
A 
309
−19.982
52.645
27.343
1.00
57.35


ATOM
1800
CD1
ILE
A 
309
−19.806
55.182
29.090
1.00
70.09


ATOM
1801
N
PHE
A
310
−22.499
51.257
25.906
1.00
46.64


ATOM
1802
CA
PHE
A
310
−22.361
49.971
25.205
1.00
44.69


ATOM
1803
C
PHE 
A
310
−22.802 
50.047
23.744
1.00
46.18


ATOM
1804
O
PHE 
A
310
−22.213
49.407
22.878
1.00
44.43


ATOM
1805
CB
PHE 
A
310
−23.069
48.828
25.946
1.00
46.18


ATOM
1806
CG
PHE 
A
310
−24.354
49.232
26.609
1.00
47.70


ATOM
1807
CD1
PHE 
A
310
−25.567
49.078
25.952
1.00
51.45


ATOM
1808
CD2
PHE 
A
310
−24.357
49.717
2.7.905 
1.00
49.97


ATOM
1809
CE1
PHE 
A
310
−26.761
49.436
26.564
1.00
52.42


ATOM
1810
CE2
PHE
A
310
−25.544
50.078
28.527
1.00
53.08


ATOM
1811
CZ
PHE
A
310
−26.752
49.929
27.854
1.00
51.29


ATOM
1812
N
GLU
A
311
−23.817
50.857
23.472
1.00
43.03


ATOM
1813
CA
GLU
A
311
−24.305
51.041
22.101
1.00
42.77


ATOM
1814
C
GLU
A
311
−23.200
51.875
21.322
1.00
45.59


ATOM
1815
O
GLU
A
311
−22.963
51.572
20.176
1.00
44.69


ATOM
1816
CB
GLU
A
311
−25.664
51.741
22.119
1.00
44.30


ATOM
1817
CG
GLU
A
311
−26.746
50.964
22.870
1.00
54.76


ATOM
1818
CD
GLU
A
311
−27.945
51.828
23.244
1.00
71.29


ATOM
1819
OE1
GLU
A
311
−27.795
53.065
23.306
1.00
62.64


ATOM
1820
OE2
GLU
A
311
−29.030
51.265
23.491
1.00
62.80


ATOM
1821
N
LEU
A
312
−22.793
52.908
21.976
1.00
42.45


ATOM
1822
CA
LEU
A
312
−21.797
53.768
21.383
1.00
42.51


ATOM
1823
C
LEU
A
312
−20.583
52.940
20.924
1.00
46.58


ATOM
1824
O
LEU
A
312
−20.150
53.029
19.771
1.00
46.36


ATOM
1825
CB
LEU
A
312
−21.368
54.814
22.412
1.00
42.78


ATOM
1826
CG
LEU
A
312
−20.790 
56.116
21.887
1.00
47.55


ATOM
1827
CD1
LEU
A
312
−20.374
56.990
23.066
1.00
47.28


ATOM
1828
CD2
LEU
A
312
−19.610
55.823
20.981
1.00
50.44


ATOM
1829
N
LEU
A
313
−20.058 
52.110
21.820
1.00
42.46


ATOM
1830
CA
LEU
A
313
−18.904
51.278
21.481
1.00
41.95


ATOM
1831
C
LEU
A
313
−19.233 
50.306
20.345
1.00
44.63


ATOM
1832
O
LEU
A
313
−18.397
50.025
19.495
1.00
43.26


ATOM
1833
CB
LEU
A
313
−18.378 
50.538
22.723
1.00
41.76


ATOM
1834
CG
LEU
A
313
−18.056 
51.464
23.900
1.00
45.89


ATOM
1835
CD1
LEU
A
313
−17.488
50.699
25.073
1.00
45.61


ATOM
1836
CD2
LEU
A
313
−17.092
52.571
23.462
1.00
48.84


ATOM
1837
N
ASP
A
314
−20.462 
49.812
20.329 
1.00
42.55


ATOM
1838
CA
ASP
A
314
−20.900 
48.920
19.261
1.00
42.99


ATOM
1839
C
ASP
A
314
−20.916 
49.684
17.931
1.00
47.01


ATOM
1840
O
ASP
A
314
−20.417 
49.199
16.920
1.00
47.11


ATOM
1841
CB
ASP
A
314
−22.288 
48.372
19.562 
1.00
45.41


ATOM
1842
CG
ASP
A
314
−22.696 
47.275
18.602
1.00
60.70


ATOM
1843
OD1
ASP
A
314
−21.841
46.430
18.269
1.00
61.48


ATOM
1844
OD2
ASP
A
314
−23.865
47.271
18.163
1.00
70.17


ATOM
1845
N
TYR
A
315
−21.464 
50.895
17.960
1.00
43.63


ATOM
1846
CA
TYR
A
315
−21.517
51.762
16.778
1.00
43.64


ATOM
1847
C
TYR
A
315
−20.119 
51.954
16.208
1.00
46.45


ATOM
1848
O
TYR
A
315
−19.885 
51.728
15.023
1.00
46.41


ATOM
1849
CB
TYR
A
315
−22.117
53.131
17.151
1.00
45.86


ATOM
1850
CG
TYR
A
315
−22.630
53.936
15.960
1.00
49.31


ATOM
1851
CD1
TYR
A
315
−21.780
54.766
15.234
1.00
51.35


ATOM
1852
CD2
TYR
A
315
−23.963
53.848
15.556
1.00
50.62


ATOM
1853
CE1
TYR
A
315
−22.236
55.486
14.141
1.00
52.66


ATOM
1854
CE2
TYR
A
315
−24.434
54.568
14.456
1.00
91.60


ATOM
1855
CZ
TYR
A
315
−23.569
55.388
13.759
1.00
59.64


ATOM
1856
OH
TYR
A
315
−24.030
56.107
12.669
1.00
60.21


ATOM
1857
N
ILE
A
316
−19.184
52.363
17.066
1.00
41.52


ATOM
1858
CA
ILE
A
316
−17.806
52.593
16.648
1.00
40.92


ATOM
1859
C
ILE
A
316
−17.229
51.358
15.964
1.00
44.59


ATOM
1860
O
ILE
A
316
−16.472
51.464
14.996
1.00
42.91


ATOM
1861
CB
ILE
A
316
−16.910
52.972
17.856
1.00
44.02


ATOM
1862
CG1
ILE
A
316
−17.305
54.359
15.400
1.00
44.48


ATOM
1863
CG2
ILE
A
316
−15.425
52.901
17.477
1.00
43.74


ATOM
1864
CD1
ILE
A
316
−16.822
54.635
19.814
1.00
47.18


ATOM
1865
N
VAL
A
317
−17.577
50.183
16.475
1.00
41.43


ATOM
1866
CA
VAL
A
317
−17.058
48.949
15.910
1.00
40.89


ATOM
1867
C
VAL
A
317
−17.739
48.547
14.613
1.00
44.22


ATOM
1868
O
VAL
A
317
−17.094
48.053
13.708 
1.00
44.19


ATOM
1869
CB
VAL
A
317
−17.151
47.757
16.918
1.00
44.34


ATOM
1870
CG1
VAL
A
317
−16.682
46.450
16.242
1.00
44.07


ATOM
1871
CG2
VAL
A
317
−16.308
48.039
18.156
1.00
43.79


ATOM
1872
N
ASN
A
318
−19.045
48.757
14.529
1.00
40.40


ATOM
1873
CA
ASN
A
318
−19.800
48.282
13.371
1.00
40.57


ATOM
1874
C
ASN
A
318
−20.216
49.270
12.292
1.00
44.87


ATOM
1875
O
ASN
A
318
−20.663
48.858
11.224
1.00
44.87


ATOM
1876
CB
ASN
A
318
−20.988
47.435
13.823
1.00
39.31


ATOM
1877
CG
ASN
A
318
−20.562
46.280
14.683
1.00
53.13


ATOM
1878
OD1
ASN
A
318
−19.736
45.463
14.268
1.00
51.50


ATOM
1879
ND2
ASN
A
318
−20.972
46.301
15.933
1.00
42.17


ATOM
1880
N
GLU
A
319
−20.084
50.563
12.566
1.00
40.57


ATOM
1881
CA
GLU
A
319
−20.462
51.579
11.595 
1.00
39.79


ATOM
1882
C
GLU
A
319
−19.237
52.212
10.954
1.00
43.04


ATOM
1883
O
GLU
A
319
−18.118
52.041
11.434
1.00
41.89


ATOM
1854
CB
GLU
A
319
−21.327
52.659
12.257
1.00
40.96


ATOM
1885
CG
GLU
A
319
−22.703
52.159
12.706 
1.00
49.50


ATOM
1886
CD
GLU
A
319
−23.481
51.475
11.578 
1.00
71.27


ATOM
1887
OE1
GLU
A
319
−23.642
52.086
10.501
1.00
65.80


ATOM
1888
OE2
GLU
A
319
−23.928
50.326
11.770
1.00
64.37


ATOM
1889
N
PRO
A
320
−19.453
52.947
9.862
1.00
39.92


ATOM
1890
CA
PRO
A
320
−18.355
53.657
9.201
1.00
38.89


ATOM
1891
C
PRO
A
320
−17.930
54.815
10.108
1.00
39.68


ATOM
1892
O
PRO
A
320
−18.745
55.360
10.861 
1.00
38.12


ATOM
1893
CB
PRO
A
320
−19.004
54.185
7.917
1.00
40.65


ATOM
1894
CG
PRO
A
320
−20.125
53.209
7.649
1.00
45.36


ATOM
1895
CD
PRO
A
320
−20.659
52.887
9.016
1.00
40.77


ATOM
1896
N
PRO
A
321
−16.649
55.158
10.068
1.00
35.12


ATOM
1897
CA
PRO
A
321
−16.109
56.207
10.939
1.00
34.70


ATOM
1898
C
PRO
A
321
−16.728
57.601
10.686 
1.00
38.34


ATOM
1899
O
PRO
A
321
−17.194
57.899
9.595
1.00
36.95


ATOM
1900
CB
PRO
A
321
−14.619
56.209
10.591
1.00
35.89


ATOM
1901
CG
PRO
A
321
−14.572
55.771
9.174
1.00
40.30


ATOM
1902
CD
PRO
A
321
−15.711
54.797
8.985
1.00
35.37


ATOM
1903
N
PRO
A
322
−16.708
58.447
11.711
1.00
35.15


ATOM
1904
CA
PRO
A
322
−17.221
59.810
11.578
1.00
34.54


ATOM
1905
C
PRO
A
322
−16.390
50.583
10.549
1.00
36.66


ATOM
1906
O
PRO
A
322
−15.270
60.190
10.193
1.00
35.07


ATOM
1907
CB
PRO
A
322
−17.040
60.406
12.987
1.00
36.06


ATOM
1908
CG
PRO
A
322
−16.099
59.490
13.678
1.00
40.17


ATOM
1909
CD
PRO
A
322
−16.280
58.147
13.086 
1.00
35.02


ATOM
1910
N
LYS
A
323
−16.958
61.667
10.065 
1.00
33.12


ATOM
1911
CA
LYS
A
323
−16.328
62.472
9.038
1.00
33.60


ATOM
1912
C
LYS
A
323
−16.685
63.935
9.297
1.00
37.57


ATOM
1913
O
LYS
A
323
−17.763
64.212
9.810
1.00
37.81


ATOM
1914
CB
LYS
A
323
−16.956
62.059
7.699
1.00
36.56


ATOM
1915
CG
LYS
A
323
−16.117
62.255
6.493
1.00
57.81


ATOM
1916
CD
LYS
A
323
−16.975
61.980
5.265
1.00
67.60


ATOM
1917
CE
LYS
A
323
−18.323
61.394
5.679
1.00
72.41


ATOM
1918
NZ
LYS
A
323
−19.471
62.120
5.063
1.00
79.18


ATOM
1919
N
LEU
A
324
−15.830
64.868
8.866
1.00
32.78


ATOM
1920
CA
LEU
A
324
−16.173
66.289
8.960
1.00
31.77


ATOM
1921
C
LEU
A
324
−17.234
66.562
7.905
1.00
37.59


ATOM
1922
O
LEU
A
324
−17.251
65.908
6.849
1.00
37.73


ATOM
1923
CB
LEU
A
324
−14.930
67.176
8.639
1.00
31.06


ATOM
1924
CG
LEU
A
324
−13.832
67.241
9.672
1.00
34.82


ATOM
1925
CD1
LEU
A
324
−12.614
67.968
9.100
1.00
34.02


ATOM
1926
CD2
LEU
A
324
−14.331
67.875 
10.988
1.00
36.00


ATOM
1927
N
PRO
A
325
−18.075
67.570
8.141
1.00
34.87


ATOM
1928
CA
PRO
A
325
−19.073
67.952
7.152
1.00
34.21


ATOM
1929
C
PRO
A
325
−18.352
68.637
5.991
1.00
38.30


ATOM
1930
O
PRO
A
325
−17.382
69.376
6.193
1.00
37.32


ATOM
3931
CB
PRO
A
325
−19.944
68.967
7.905
1.00
35.96


ATOM
1932
CG
PRO
A
325
−19.163
69.313
9.150
1.00
40.54


ATOM
1933
CD
PRO
A
325
−18.391
66.115
9.469
1.00
35.53


ATOM
1934
N
SER
A
326
−18.805
68.376
4.777
1.00
36.40


ATOM
1935
CA
SER
A
326
−18.173
68.962
3.605
1.00
36.90


ATOM
1936
C
SER
A
326
−18.557
70.426
3.461
1.00
42.28


ATOM
1937
O
SER
A
226
−19.500
70.892
4.094
1.00
42.77


ATOM
1938
CB
SER
A
326
−18.554
68.183
2.348
1.00
40.98


ATOM
1939
OG
SER
A
326
−19.892
68.429
1.986
1.00
50.24


ATOM
1940
N
GLY
A
327
−17.807
71.156
2.648.
1.00
39.14


ATOM
1941
CA
GLY
A
327
−18.121
72.563
2.375
1.00
39.60


ATOM
1942
C
GLY
A
327
−17.789
73.598
3.466
1.00
44.11


ATOM
1943
O
GLY
A
327
−17.784
74.797
3.195
1.00
45.55


ATOM
1944
N
VAL
A
328
−17.535
73.153
4.690
1.00
38.22


ATOM
1945
CA
VAL
A
328
−17.236
74.102
5.771
1.00
36.90


ATOM
1946
C
VAL
A
328
−15.800
74.010
6.249
1.00
37.52


ATOM
1947
O
VAL
A
328
−15.292
74.910
6.919
1.00
36.02


ATOM
1948
CB
VAL
A
328
−18.234
73.991
6.946
1.00
40.77


ATOM
1949
CG1
VAL
A
328
−19.589
74.481
6.511
1.00
40.46


ATOM
1950
CG2
VAL
A
328
−18.327
72.568
7.441
1.00
40.61


ATOM
1951
N
PHE
A
329
−15.135
72.921
5.862
1.00
31.60


ATOM
1952
CA
PHE
A
329
−12.733
72.708
6.202
1.00
29.58


ATOM
1953
C
PHE
A
329
−12.980
72.434
4.902
1.00
31.56


ATOM
1954
O
PHE
A
329
−13.566
71.934
3.945
1.00
29.09


ATOM
1955
CB
PHE
A
329
−13.613
71.513
7.149
1.00
30.71


ATOM
1956
CG
PHE
A
329
−14.246
71.751
8.495
1.00
31.66


ATOM
1957
CD1
PHE
A
329
−13.597
72.523
9.453
1.00
33.13


ATOM
1958
CD2
PHE
A
329
−15.515
71.252
8.786
1.00
33.12


ATOM
1959
CE1
PHE
A
329
−14.170
72.763
10.677
1.00
33.81


ATOM
1960
CE2
PHE
A
329
−16.113
71.516
10.013
1.00
35.49


ATOM
1961
CZ
PHE
A
329
−15.433
72.259
10.962
1.00
33.57


ATOM
1962
N
SER
A
330
−11.679
72.735
4.876
1.00
26.61


ATOM
1963
CA
SER
A
330
−10.894
72.490
3.679
1.00
24.60


ATOM
1964
C
SER
A
330
−10.857
70.995
3.368
1.00
31.01


ATOM
1965
O
SER
A
330
−11.039
70.160
4.248
1.00
30.95


ATOM
1966
CB
SER
A
330
−9.473
73.057
3.798
1.00
23.12


ATOM
1967
OG
SER
A
330
−8.667
72.262
4.659
1.00
27.45


ATOM
1968
N
LEU
A
331
−10.664
70.668
2.100
1.00
28.50


ATOM
1969
CA
LEU
A
331
−10.577
69.279
1.683
1.00
27.67


ATOM
1970
C
LEU
A
331
−9.361
68.642
2.326
1.00
31.77


ATOM
1971
O
LEU
A
331
−9.382
67.463
2.675
1.00
31.97


ATOM
1972
CB
LEU
A
331
−10.478
69.199
0.168
1.00
27.84


ATOM
1973
CG
LEU
A
331
−11.800
69.462
−0.559
1.00
33.09


ATOM
1974
CD1
LEU
A
331
−11.648
69.210
−2.054
1.00
33.00


ATOM
1975
CD2
LEU
A
331
−12.864
68.546
0.040
1.00
36.48


ATOM
1976
N
GLU
A
332
−8.296
69.432
2.498
1.00
28.00


ATOM
1977
CA
GLU
A
332
−7.060
68.935
3.136
1.00
27.28


ATOM
1978
C
GLU
A
332
−7.278
68.529
4.576
1.00
30.11


ATOM
1979
O
GLU
A
332
−6.782
67.471
5.019
1.00
30.82


ATOM
1980
CB
GLU
A
332
−5.940
69.969
3.038
1.00
29.00


ATOM
1981
CG
GLU
A
332
−5.441
70.144
1.598
1.00
38.55


ATOM
1982
CD
GLU
A
332
−4.458
71.272
1.444
1.00
46.99


ATOM
1983
OE1
GLU
A
332
−4.484
72.197
2.273
1.00
41.37


ATOM
1984
OE2
GLU
A
332
−3.694
71.260
0.455
1.00
38.31


ATOM
1985
N
PHE
A
333
−8.021
69.352
5.319
1.00
24.30


ATOM
1986
CA
PHE
A
333
−8.341
69.012
6.723
1.00
23.92


ATOM
1987
C
PHE
A
333
−9.222
67.756
6.733
1.00
27.77


ATOM
1988
O
PHE
A
333
−8.987
66.836
7.503
1.00
27.02


ATOM
1989
CB
PHE
A
333
−9.091
70.167
7.423
1.00
25.34


ATOM
1990
CG
PHE
A
333
−9.321 
69.936
8.903
1.00
26.39


ATOM
1991
CD1
PHE
A
333
−8.435
69.142
9.651
1.00 
28.35


ATOM
1992
CD2
PHE
A
333
−10.405
70.523
9.554
1.00
27.27


ATOM
1993
CE1
PHE
A
333
−8.622
68.951
11.012
1.00
28.73


ATOM
1994
CE2
PHE
A
333
−10.617
70.318
10.907
1.00
29.37


ATOM
1995
CZ
PHE
A
333
−9.723
69.538
11.643
1.00
27.96


ATOM
1996
N
GLN
A
334
−10.211
67.715
5.841
1.00
25.99


ATOM
1997
CA
GLN
A
334
−11.115
66.552
5.740
1.00
26.52


ATOM
1998
C
GLN
A
334
−10.347
65.262
5.427
1.00
30.07


ATOM
1999
O
GLN
A
334
−10.600
64.199
6.020
1.00
30.62


ATOM
2000
CB
GLN
A
334
−12.179
66.784
4.652
1.00
27.69


ATOM
2001
CG
GLN
A
334
−13.232
67.844
4.977
1.00
25.79


ATOM
2002
CD
GLN
A
334
−14.139
68.144
3.765
1.00
31.23


ATOM
2003
OE1
GLN
A
334
−14.851
67.273
3.284
1.00
30.92


ATOM
2004
NE2
GLN
A
334
−14.039
69.350
3.232
1.00
23.72


ATOM
2005
N
ASP
A
335
−9.428
65.350
4.483
1.00
26.02


ATOM
2006
CA
ASP
A
335
−8.648
64.194
4.093
1.00
26.09


ATOM
2007
C
ASP
A
335
−7.777
63.749
5.274
1.00
30.81


ATOM
2008
O
ASP
A
335
−7.656
62.553
5.554
1.00
30.96


ATOM
2009
CB
ASP
A
335
−7.786
64.522
2.872
1.00
27.46


ATOM
2010
CG
ASP
A
335
−6.974
63.319
2.380
1.00
32.21


ATOM
2011
OD1
ASP
A
335
−7.592
62.349
1.873
1.00
31.78


ATOM
2012
OD2
ASP
A
335
−5.721
63.387
2.436
1.00
33.06


ATOM
2013
N
PHE
A
336
−7.175
64.722
5.959
1.00
26.96


ATOM
2014
CA
PHE
A
336
−6.342
64.448
7.132
1.00
26.35


ATOM
2015
C
PHE
A
336
−7.114
63.640
8.176
1.00
27.67


ATOM
2016
O
PHE
A
336
−6.651
62.619
8.637
1.00
27.52


ATOM
2017
CB
PHE
A
336
−5.853
55.765
7.765
1.00
28.36


ATOM
2018
CG
PHE
A
336
−4.995
65.565
8.990
1.00
30.33


ATOM
2019
CD1
PHE
A
335
−3.632
65.300
8.866
1.00
33.04


ATOM
2020
CD2
PHE
A
336
−5.546
65.654
10.259
1.00
31.38


ATOM
2021
CE1
PHE
A
336
−2.843
65.115
9.987
1.00
33.46


ATOM
2022
CE2
PHE
A
336
−4.759
65.472
11.388
1.00
34.10


ATOM
2023
CZ
PHE
A
336
−3.411
65.219
11.256
1.00
32.40


ATOM
2024
N
VAL
A
337
−8.291
64.124
8.561
1.00
24.17


ATOM
2025
CA
VAL
A
337
−9.085
63.414
9.547
1.00
25.29


ATOM
2026
C
VAL
A
337
−9.518
62.052
9.018
1.00
29.79


ATOM
2027
O
VAL
A
337
−9.539
61.091
9.757
1.00
27.98


ATOM
2028
CB
VAL
A
337
−10.324
64.227
10.044
1.00
30.06


ATOM
2029
CG1
VAL
A
337
−9.887
65.549
10.707
1.00
29.67


ATOM
2030
CG2 
VAL
A
337
−11.282
64.475
8.930
1.00
30.23


ATOM
2031
N
ASN
A
338
−9.823
61.978
7.718
1.00
28.40


ATOM
2032
CA
ASN
A
338
−10.230
60.712
7.087
1.00
28.63


ATOM
2033
C
ASN
A
338
−9.147
59.652
7.210
1.00
32.34


ATOM
2034
O
ASN
A
338
−9.431
58.493
7.555
1.00
31.89


ATOM
2035
CB
ASN
A
338
−10.584
60.922
5.602
1.00
27.32


ATOM
2036
CG
ASN
A
338
−11.990
61.482
5.417
1.00
37.97


ATOM
2037
OD1
ASN
A
338
−12.745
61.597
6.372
1.00
33.44


ATOM
2038
ND2
ASN
A
338
−12.346 
61.794
4.193
1.00
27.86


ATOM
2039
N
LYS
A
339
−7.907
60.041
6.944
1.00
27.59


ATOM
2040
CA
LYS
A
339
−6.799
59.088
7.022
1.00
27.37


ATOM
2041
C
LYS
A
339
−6.510
58.629
8.455
1.00
31.39


ATOM
2042
O
LYS
A
339
−5.948
57.549
8.668
1.00
30.68


ATOM
2043
CB
LYS
A
339
−5.544
59.669
6.369
1.00
29.65


ATOM
2044
CG
LYS
A
339
−5.572 
59.625
4.839
1.00
28.82


ATOM
2045
CD
LYS
A
339
−4.441
60.467
4.252
1.00
37.12


ATOM
2046
CE
LYS
A
339
−4.127
60.046
2.819
1.00
36.67


ATOM
2047
NZ
LYS
A
339
−5.175
60.509
1.869
1.00
36.80


ATOM
2048
N
CYS
A
340
−6.910
59.443
9.433
1.00
28.17


ATOM
2049
CA
CYS
A
340
−6.694
59.106
10.845
1.00
28.24


ATOM
2050
C
CYS
A
340
−7.781
58.154
11.286
1.00
32.62


ATOM
2051
O
CYS
A
340
−7.627
57.431
12.258
1.00
31.48


ATOM
2052
CB
CYS
A
340
−6.808
60.371
11.733
1.00
28.31


ATOM
2053
SG
CYS
A
340
−5.410
61.517
11.689
1.00
31.92


ATOM
2054
N
LEU
A
341
−8.926
58.255
10.628
1.00
30.59


ATOM
2055
CA
LEU
A
341
−10.102
57.521
11.041
1.00
31.20


ATOM
2056
C
LEU
A
341
−10.418
56.228
10.278
1.00
35.98


ATOM
2057
O
LEU
A
341
−11.455
55.631
10.494
1.00
36.00


ATOM
2058
CB
LEU
A
341
−11.310
58.450
11.068
1.00
30.96


ATOM
2059
CG
LEU
A
341
−11.231
59.543
12.155
1.00
35.51


ATOM
2060
CD1
LEU
A
341
−12.466
60.441
12.134
1.00
35.08


ATOM
2061
CD2
LEU
A
341
−11.060
58.923
13.528
1.00
37.81


ATOM
2062
N
ILE
A
342
−9.530
55.815
9.387
1.00
34.11


ATOM
2063
CA
ILE
A
342
−9.734
54.565
8.650
1.00
35.01


ATOM
2064
C
ILE
A
342
−9.748
53.418
9.681
1.00
41.39


ATOM
2065
O
ILE
A
342
−8.825
53.285
10.470
1.00
41.24


ATOM
2066
CB
ILE
A
342
−8.618
54.351
7.620
1.00
37.83


ATOM
2067
CG1
ILE
A
342
−8.830
55.279
6.416
1.00
27.19


ATOM
2068
CG2
ILE
A
342
−8.534
52.862
7.192
1.00
38.50


ATOM
2069
CD1
ILE
A
342
−7.588
55.618
5.688
1.00
40.07


ATOM
2070
N
LYS
A
343
−10.851
52.677
9.736
1.00
39.60


ATOM
2071
CA
LYS
A
343
−11.015
51.595
10.717
1.00
39.73


ATOM
2072
C
LYS
A
343
−9.906
50.556
10.696
1.00
44.18


ATOM
2073
O
LYS
A
343
−9.505
50.046
11.737
1.00
43.81


ATOM
2074
CB
LYS
A
343
−12.369
50.927
10.558
1.00
42.27


ATOM
2075
CG
LYS
A
343
−13.533
51.891
10.607
1.00
48.55


ATOM
2076
CD
LYS
A
343
−14.533
51.478
11.665
1.00
51.80


ATOM
2077
CE
LYS
A
343
−15.684
50.713
11.056
1.00
51.26


ATOM
2078
NZ
LYS
A
343
−16.428
49.969
12.086
1.00
57.44


ATOM
2079
N
ASN
A
344
−9.408
50.242
9.512
1.00
41.64


ATOM
2080
CA
ASN
A
344
−8.313
49.284
9.385
1.00
41.45


ATOM
2081
C
AEN
A
344
−6.995
49.970
9.760
1.00
43.89


ATOM
2082
O
ASN
A
344
−6.499
50.816
9.018
1.00
43.59


ATOM
2083
CB
ASN
A
344
−8.238
48.752
7.949
1.00
42.23


ATOM
2084
CG
ASN
A
344
−7.166
47.701
7.777
1.00 
63.68


ATOM
2085
OD1
ASN
A
344
−6.364
47.465
8.678
1.00
53.64


ATOM
2086
ND2
ASN
A
344
−7.135
47.073
6.606
1.00
57.56


ATOM
2087
N
PRO
A
345
−6.428
49.593
10.901
1.00
39.46


ATOM
2088
CA
PRO
A
345
−5.204
50.226
11.386
1.00
39.26


ATOM
2089
C
PRO
A
345
−4.048
50.170
10.402
1.00
45.38


ATOM
2090
O
PRO
A
345
−3.154
51.021
10.443
1.00
44.10


ATOM
2091
CB
PRO
A
345
−4.867
49.432
12.680
1.00
40.47


ATOM
2092
CG
PRO
A
345
−5.859
48.286
12.727
1.00
44.59


ATOM
2093
CD
PRO
A
345
−7.040
48.728
11.923
1.00
39.86


ATOM
2094
N
ALA
A
346
−4.049
49.151
9.535
1.00
43.85


ATOM
2095
CA
ALA
A
346
−2.980
48.979
8.546
1.00
43.74


ATOM
2096
C
ALA
A
346
−3.069
50.012
7.425
1.00
46.66


ATOM
2097
O
ALA
A
346
−2.052
50.463
6.897
1.00
46.97


ATOM
2098
CB
ALA
A
345
−3.008
47.565
7.972
1.00
44.71


ATOM
2099
N
GLU
A
347
−4.292
50.394
7.076
1.00
41.94


ATOM
2100
CA
GLU
A
347
−4.514
51.372
6.017
1.00
40.97


ATOM
2101
C
GLU
A
347
−4.501
52.801
6.596
1.00
42.16


ATOM
2102
O
GLU
A
347
−4.085
53.739
5.932
1.00
40.74


ATOM
2103
CB
GLU
A
347
−5.836
51.081
5.296
1.00
42.54


ATOM
2104
CG
GLU
A
347
−5.725
49.987
4.242
1.00
55.16


ATOM
2105
CD
GLU
A
347
−4.430
50.073
3.447
1.00
74.37


ATOM
2106
OE1
GLU
A
347
−4.238 
51.080
2.730 
1.00
67.13


ATOM
2107
OE2
GLU
A
347
−3.593
49.149
3.564 
1.00
66.32


ATOM
2108
N
ARG
A
348
−4.940 
52.934
7.848
1.00
37.66


ATOM
2109
CA
ARG
A
348
−4.913
54.212
8.566 
1.00
36.75


ATOM
2110
C
ARG
A
348
−3.498
54.776
8.470 
1.00
41.20


ATOM
2111
O
ARG
A
348
−2.529
54.032
8.546
1.00
41.88


ATOM
2112
CB
ARG
A
348
−5.263
53.966
10.042
1.00
34.15


ATOM
2113
CG
ARG
A
348
−5.359
55.209
10.899
1.00
34.44


ATOM
2114
CD
ARG
A
348
−5.726 
54.852
12.338 
1.00
34.00


ATOM
2115
NE
ARG
A
348
−6.909
53.982
12.414
1.00
35.16


ATOM
2116
CZ
ARG
A
348
−7.072
53.025
13.328
1.00
46.14


ATOM
2117
NH1
ARG
A
348
−6.145
52.841
14.263
1.00
33.01


ATOM
2118
NH2
ARG
A
348
−8.162
52.267
13.323
1.00
32.43


ATOM
2119
N
ALA
A
349
−3.370 
56.064
8.287
1.00
37.20


ATOM
2120
CA
ALA
A
349
−2.039
56.686
8.179
1.00
36.49


ATOM
2121
C
ALA
A
349
−1.228
56.559
9.474
1.00
39.33


ATOM
2122
O
ALA
A
349
−1.794 
56.423
10.565
1.00
38.24


ATOM
2123
CB
ALA
A
349
−2.139 
58.146
7.741
1.00
37.24


ATOM
2124
N
ASP
A
350
0.097
56.587
9.347
1.00
35.64


ATOM
2125
CA
ASP
A
350
0.966
56.513
10.520
1.00
35.83


ATOM
2126
C
ASP
A
350
1.556
57.892
10.836 
1.00
38.79


ATOM
2127
O
ASP
A
350
1.326
58.848
10.097
1.00
38.55


ATOM
2128
CB
ASP
A
350
2.066
55.434
10.360
1.00
37.60


ATOM
2129
CG
ASP
A
350
3.030
55.725
9.215
1.00
48.16


ATOM
2130
OD1
ASP
A
350
3.044
56.860
8.708
1.00
47.70


ATOM
2131
OD2
ASP
A
350
3.793
54.806
8.833
1.00
56.18


ATOM
2132
N
LEU
A
351
2.264
58.002
11.955
1.00
34.11


ATOM
2133
CA
LEU
A
351
2.834
59.286
12.364
1.00
33.95


ATOM
2134
C
LEU
A
351
3.722
59.907
11.309
1.00
38.84


ATOM
2135
O
LEU
A
351
3.692
61.125
11.093
1.00
39.22


ATOM
2136
CB
LEU
A
351
3.585
59.166
13.702
1.00
33.75


ATOM
2137
CG
LEU
A
351
2.735
58.919
14.958
1.00
38.08


ATOM
2138
CD1
LEU
A
351
3.611
58.519
16.137
1.00
38.20


ATOM
2139
CD2
LEU
A
351
1.884
60.147
15.306
1.00
38.11


ATOM
2140
N
LYS
A
352
4.520
59.076
10.650
1.00
36.22


ATOM
2141
CA
LYS
A
352
5.437
59.560
9.606
1.00
35.76


ATOM
2142
C
LYS
A
352
4.671
60.151
8.447
1.00
37.55


ATOM
2143
O
LYS
A
352
5.030
61.191
7.918
1.00
37.07


ATOM
2144
CB
LYS
A
352
6.319
58.410
9.102
1.00
39.45


ATOM
2145
CG
LYS
A
352
7.273
58.791
7.993
1.00
56.87


ATOM
2146
CD
LYS
A
352
8.661
58.190
8.242
1.00
68.69


ATOM
2147
CE
LYS
A
352
9.582
58.400
7.057
1.00
77.61


ATOM
2148
NZ
LYS
A
352
10.302
59.700
7.146
1.00
88.34


ATOM
2149
N
GLN
A
353
3.609
59.476
8.038
1.00
33.86


ATOM
2150
CA
GLN
A
353
2.819
59.955
6.906
1.00
33.54


ATOM
2151
C
GLN
A
353
2.061
61.245
7.275
1.00
36.10


ATOM
2152
O
GLN
A
353
1.992
62.189
6.489
1.00
35.26


ATOM
2153
CB
GLN
A
353
1.854
58.867
6.438
1.00
34.74


ATOM
2154
CG
GLN
A
353
2.560
57.561
6.041
1.00
45.86


ATOM
2155
CD
GLN
A
353
1.593
56.408
5.800
1.00
62.98


ATOM
2156
OE1
GLN
A
353
0.505
56.368
6.362
1.00
55.37


ATOM
2157
NE2
GLN
A
353
2.004
55.457
4.971
1.00
61.58


ATOM
2158
N
LEU
A
354
1.526
61.279
8.491
1.00
32.23


ATOM
2159
CA
LEU
A
354
0.785
62.458
8.980
1.00
31.60


ATOM
2160
C
LEU
A
354
1.660
63.679
9.032
1.00
34.51


ATOM
2161
O
LEU
A
354
1.263
64.741
8.594
1.00
33.34


ATOM
2162
CB
LEU
A
354
0.188
62.173
10.345
1.00
31.29


ATOM
2163
CG
LEU
A
354
−0.977
61.194
10.251
1.00
35.33


ATOM
2164
CD1
LEU
A
354
−1.534
60.864
11.640
1.00
34.91


ATOM
2165
CD2
LEU
A
354
−2.075
61.769
9.332
1.00
36.32


ATOM
2166
N
MET
A
355
2.888
63.502
9.502
1.00
33.82


ATOM
2167
CA
MET
A
355
3.845
64.605
9.610
1.00
34.83


ATOM
2168
C
MET
A
355
4.054
65.341
8.290
1.00
36.88


ATOM
2169
O
MET
A
355
4.3.62
66.532
8.275
1.00
36.04


ATOM
2170
CB
MET
A
355
5.189
64.103
10.154
1.00
38.16


ATOM
2171
CG
MET
A
355
5.388
64.326
11.667
1.00
43.32


ATOM
2172
SD
MET
A
355
5.398
66.080
12.133
1.00
48.91


ATOM
2173
CE
MET
A
355
3.798
66.313
12.705
1.00
46.14


ATOM
2174
N
VAL
A
356
3.899
64.630
7.180
1.00
32.88


ATOM
2175
CA
VAL
A
355
4.054
65.251
5.876
1.00
32.76


ATOM
2176
C
VAL
A
356
2.735
65.374
5.110
1.00
34.11


ATOM
2177
O
VAL
A
356
2.714
65.756
3.945
1.00
32.61


ATOM
2178
CB
VAL
A
356
5.133
64.571
5.039
1.00
37.75


ATOM
2179
CG1
VAL
A
356
6.524
64.840
5.664
1.00
37.83


ATOM
2180
CG2
VAL
A
356
4.860
63.052
4.922
1.00
37.35


ATOM
2181
N
HIS
A
357
1.623
65.104
5.791
1.00
29.28


ATOM
2182
CA
HIS
A
357
0.326
65.263
5.147
1.00
27.92


ATOM
2183
C
HIS
A
357
0.140
66.732
4.718
1.00
31.01


ATOM
2184
O
HIS
A
357
0.618
67.648
5.386
1.00
30.34


ATOM
2185
CB
HIS
A
357
−0.804
64.836
6.090
1.00
28.13


ATOM
2186
CG
HIS
A
357
−2.145
64.829
5.441
1.00
31.16


ATOM
2187
ND1
HIS
A
357
−2.857
65.988
5.192
1.00
31.95


ATOM
2188
CD2
HIS
A
357
−2.872
63.815
4.909
1.00
32.33


ATOM
2189
CE1
HIS
A
357
−3.974
65.681
4.558
1.00
31.29


ATOM
2190
NE2
HIS
A
357
−4.017
64.369
4.390
1.00
31.70


ATOM
2191
N
ALA
A
358
−0.551
66.946
3.603
1.00
27.16


ATOM
2192
CA
ALA
A
358
−0.800
68.295
3.092
1.00
26.83


ATOM
2193
C
ALA
A
358
−1.333
69.262
4.165
1.00
31.83


ATOM
2194
O
ALA
A
358
−0.991
70.451
4.170
1.00
31.68


ATOM
2195
CB
ALA
A
358
−1.749
68.244
1.936
1.00
27.36


ATOM
2196
N
PHE
A
359
−2.226
68.768
5.019
1.00
27.79


ATOM
2197
CA
PHE
A
359
−2.833
69.612
6.056
1.00
26.85


ATOM
2198
C
PHE
A
359
−1.801
70.061
7.106
1.00
32.35


ATOM
2199
O
PHE
A
359
−1.810
71.202
7.560
1.00
30.27


ATOM
2200
CB
PHE
A
359
−3.984
68.875
6.734
1.00
27.94


ATOM
2201
CG
PHE
A
359
−4.596
69.631
7.888
1.00
28.04


ATOM
2202
CD1
PHE
A
359
−5.221
70.840
7.681
1.00
30.15


ATOM
2203
CD2
PHE
A
359
−4.540
69.124
9.177
1.00
29.15


ATOM
2204
CE1
PHE
A
359
−5.792
71.525
8.734
1.00
30.51


ATOM
2205
CE2
PHE
A
359
−5.104
69.807
10.218 
1.00
31.51


ATOM
2206
CZ
PHE
A
359
−5.717
71.020
9.993
1.00
28.76


ATOM
2207
N
ILE
A
360
−0.917
69.148
7.485
1.00
30.94


ATOM
2208
CA
ILE
A
360
0.114
69.446
8.463
1.00
30.45


ATOM
2209
C
ILE
A
360
1.132
70.449
7.883
1.00
36.72


ATOM
2210
O
ILE
A
360
1.453
71.473
8.506
1.00
37.01


ATOM
2211
CB
ILE
A
360
0.802
68.144
8.928
1.00
32.90


ATOM
2212
CH1
ILE
A
360
−0.207
67.267
9.677
1.00
32.49


ATOM
2213
CG2
ILE
A
360
2.034
68.443
9.796
1.00
33.19


ATOM
2214
CD1
ILE
A
360
−0.983
68.023
10.778
1.00
30.76


ATOM
2215
N
LYS
A
361
1.587
70.176
6.668
1.00
33.66


ATOM
2216
CA
LYS
A
361
2.522
71.049
5.990
1.00
33.64


ATOM
2217
C
LYS
A
361
1.950
72.450
5.800
1.00
37.50


ATOM
2218
O
LYS
A
361
2.646
73.446
6.039
1.00
37.47


ATOM
2219
CB
LYS
A
361
2.954
70.443
4.655
1.00
36.32


ATOM
2220
CG
LYS
A
361
4.096
69.443
4.794
1.00
51.98


ATOM
2221
CD
LYS
A
361
3.929
68.266
3.857
1.00
63.28


ATOM
2222
CE
LYS
A
361
3.567
68.713
2.448
1.00
75.48


ATOM
2223
NZ
LYS
A
361
3.909
67.668
1.447
1.00
85.72


ATOM
2224
N
ARG
A
362
0.690
72.540
5.372
1.00
32.63


ATOM
2225
CA
ARG
A
362
0.040
73.863
5.232
1.00
31.96


ATOM
2226
C
ARG
A
362
−0.064
74.550
6.617
1.00
35.03


ATOM
2227
O
ARG
A
362
0.331
75.702
6.790
1.00
34.72


ATOM
2228
CB
ARG
A
362
−1.361
73.718
4.629
1.00
30.62


ATOM
2229
CG
ARG
A
362
−2.072
75.353
4.341
1.00
33.57


ATOM
2230
CD
ARG
A
362
−3.583
74.858
4.118
1.00
38.78


ATOM
2231
NE
ARG
A
362
−4.367
74.836
5.376
1.00
33.99


ATOM
2232
CZ
ARG
A
362
−5.534
74.206
5.520
1.00
44.26


ATOM
2233
NH1
ARG
A
362
−6.058
73.534
4.503
1.00
31.69


ATOM
2234
NH2
ARG
A
362
−6.187
74.255
6.675
1.00
31.58


ATOM
2235
N
SER
A
363
−0.588
73.821
7.599
1.00
30.47


ATOM
2236
CA
SER
A
363
−0.750
74.369
8.945
1.00
30.07


ATOM
2237
C
SER
A
363
0.578
74.862
9.535
1.00
36.06


ATOM
2238
O
SER
A
363
0.663
75.959
14.080
1.00
34.89


ATOM
2239
CB
SER
A
363
−1.408
73.325
9.868
1.00
31.36


ATOM
2240
OG
SER
A
363
−2.778
73.145
9.524
1.00
35.29


ATOM
2241
N
ASP
A
364
1.613
74.043
9.407
1.00
34.95


ATOM
2242
CA
ASP
A
364
2.932
74.382
9.929
1.00
35.73


ATOM
2243
C
ASP
A
364
3.462
75.701
9.372
1.00
41.56


ATOM
2244
O
ASP
A
364
4.194
76.411
10.046
1.00
40.90


ATOM
2245
CB
ASP
A
364
3.931
73.253
9.626
1.00
37.90


ATOM
2246
CG
ASP
A
364
4.981
73.089
10.718
1.00
52.59


ATOM
2247
OD1
ASP
A
364
4.955
73.877
11.693
1.00
55.51


ATOM
2248
OD2
ASP
A
364
5.788
72.136
10.636
1.00
56.27


ATOM
2249
N
ALA
A
365
3.099
76.016
8.131
1.00
39.67


ATOM
2250
CA
ALA
A
365
3.572
77.238
7.490
1.00
40.44


ATOM
2251
C
ALA
A
365
2.695
78.456
7.782
1.00
46.20


ATOM
2252
O
ALA
A
365
3.106
79.587
7.546
1.00
46.56


ATOM
2253
CB
ALA
A
365
3.731
77.028
5.974
1.00
41.24


ATOM
2254
N
GLU
A
366
1.486
78.226
8.294
1.00
42.84


ATOM
2255
CA
GLU
A
366
0.583
79.329
8.624
1.00
42.41


ATOM
2256
C
GLU
A
366
1.057
80.051
9.886
1.00
47.12


ATOM
2257
O
GLU
A
366
1.539
79.430
10.825
1.00
46.41


ATOM
2258
CB
GLU
A
366
−0.831
78.812
8.873
1.00
43.36


ATOM
2259
CG
GLU
A
366
−1.632
78.538
7.641
1.00
45.65


ATOM
2260
CD
GLU
A
366
−2.776
77.587
7.908
1.00
47.57


ATOM
2261
OE1
GLU
A
366
−2.990
77.202
9.083
1.00
37.93


ATOM
2262
OE2
GLU
A
366
−3.451
77.209
6.950
1.00
34.94


ATOM
2263
N
GLU
A
367
0.893
81.361
9.909
1.00
45.83


ATOM
2264
CA
GLU
A
367
1.246
82.142
11.089
1.00
46.77


ATOM
2265
C
GLU
A
367
−0.025
82.270
11.882
1.00
50.64


ATOM
2266
O
GLU
A
367
−0.884
83.087
11.555
1.00
51.21


ATOM
2267
CB
GLU
A
367
1.754
83.540
10.692
1.00
48.58


ATOM
2268
CG
GLU
A
367
2.391
84.334
11.649
1.00
62.50


ATOM
2269
CD
GLU
A
367
2.075
85.826
11.785
1.00
93.32


ATOM
2270
OE1
GLU
A
367
1.012
86.230
12.312
1.00
93.08


ATOM
2271
OE2
GLU
A
367
2.883
86.595
11.201
1.00
88.74


ATOM
2272
N
VAL
A
368
−0.198
81.387
12.859
1.00
46.08


ATOM
2273
CA
VAL
A
368
−1.414
81.379
13.658
1.00
45.39


ATOM
2274
C
VAL
A
365
−1.105
81.779
15.083
1.00
46.99


ATOM
2275
O
VAL
A
368
−0.239
81.189
15.727
1.00
45.14


ATOM
2276
CB
VAL
A
368
−2.072
79.985
13.658
1.00
49.55


ATOM
2277
CG1
VAL
A
368
−3.402
80.023
14.395
1.00
49.37


ATOM
2278
CG2
VAL
A
368
−2.255
79.489
12.248
1.00
49.42


ATOM
2279
N
ASP
A
359
−1.792
82.805
15.574
1.00
42.81


ATOM
2280
CA
ASP
A
369
−1.569
83.250
16.942
1.00
42.07


ATOM
2281
C
ASP
A
369
−2.467
82.449
17.867
1.00
43.01


ATOM
2282
O
ASP
A
369
−3.564
82.878
18.198
1.00
42.39


ATOM
2283
CB
ASP
A
369
−1.874
84.735
17.090
1.00
44.32


ATOM
2284
CG
ASP
A
369
−1.731
85.210
18.519
1.00
54.17


ATOM
2285
OD1
ASP
A
369
−0.770
84.777
19.120
1.00
52.94


ATOM
2286
OD2
ASP
A
369
−2.51.9 
85.952
12.999
1.00
64.17


ATOM
2287
N
PHE
A
370
−2.009
21.269
18.256
1.00
37.69


ATOM
2288
CA
PHE
A
373
−2.815
80.401
19.103
1.00
35.98


ATOM
2289
C
PHE
A
370
−3.065
80.998
20.469 
1.00
37.78


ATOM
2290
O
PHE
A
370
−4.187
80.968 
20.973
1.00
35.97


ATOM
2291
CB
PHE
A
370
−2.190
79.009 
19.245 
1.00
36.86


ATOM
2292
CG
PHE
A
370
−2.915
78.116 
20.224
1.00
37.28


ATOM
2293
CD1
PHE
A
370
−4.229
77.744
20.000 
1.00
40.25


ATOM
2294
CD2
PHE
A
370.
−2.300
77.676 
21.373
1.00
38.05


ATOM
2295
CE1
PHE
A
370
−4.896
76.932 
20.900
1.00
40.52


ATOM
2296
CE2
PHE
A
370
−2.962 
76.858 
22.259
1.00
40.30


ATOM
2297
CZ
PHE
A
370
−4.261
76.489 
22.020 
1.00
38.23


ATOM
2298
N
ALA
A 
371
−2.004
81.494 
21.093 
1.00
35.92


ATOM
2299
CA
ALA
A
371
−2.117
82.086 
22.430
1.00
36.20


ATOM
2300
C
ALA
A
371
−3.174 
83.179
22.457 
1.00
39.93


ATOM
2301
O
ALA
A
371
−4.017 
83.217
23.356 
1.00
41.31


ATOM
2302
CB
ALA
A
371
−0.747
82.628 
22.907 
1.00
37.21


ATOM
2303
N
GLY
A
372
−3.160
84.038
21.442 
1.00
36.63


ATOM
2304
CA
GLY
A
372
−4.134
85.139 
21.345
1.00
36.17


ATOM
2305
C
GLY
A
372
−5.555
84.618 
21.186 
1.00
39.13


ATOM
2306
O
GLY
A
372
−6.475
85.055 
21.897
1.00
39.59


ATOM
2307
N
TRP
A
373
−5.748 
83.698
20.238 
1.00
32.69


ATOM
2308
CA
TRP
A
373
−7.068
83.117
20.022
1.00
30.86


ATOM
2309
C
TRP
A
373
−7.548
82.476
21.303
1.00
33.87


ATOM
2310
O
TRP
A
373
−8.710
82.600
21.675
1.00
33.68


ATOM
2311
CB
TRP
A
373
−7.033
82.063 
18.908
1.00
28.64


ATOM
2312
CG
TRP
A
373
−8.326 
81.285 
18.805 
1.00
28.82


ATOM
2313
CD1
TRP
A
373
−9.418
81.597
18.033
1.00
31.62


ATOM
2314
CD2
TRP
A
373
−8.671
80.092
19.527
1.00
27.95


ATOM
2315
NE1
TRP
A
373
−10.416
80.667 
18.230
1.00
30.93


ATOM
2316
CE2
TRP
A
373
−9.987
79.738 
19.147 
1.00
32.21


ATOM
2317
CE3
TRP
A
373
−8.021
79.321
20.497 
1.00
28.68


ATOM
2318
CZ2
TRP
A
373
−10.653
78.629
19.695
1.00
31.13


ATOM
2319
CZ3
TRP
A
373
−8.664
78.205
21.009
1.00
29.76


ATOM
2320
CH2
TRP
A
373
−9.974 
77.884 
20.631
1.00
30.49


ATOM
2321
N
LEU
A
374
−6.649
81.747 
21.957 
1.00
30.06


ATOM
2322
CA
LEU
A
374
−6.976
81.034 
23.176
1.00
29.19


ATOM
2323
C
LEU
A
374
−7.372
81.973
24.310 
1.00
35.36


ATOM
2324
O
LEU
A
374
−8.393
81.770
24.956 
1.00
34.84


ATOM
2325
CB
LEU
A
374
−5.803
80.148 
23.621 
1.00
28.66


ATOM
2326
CG
LEU
A
374
−6.032
79.430
24.961 
1.00
32.17


ATOM
2327 
CD1
LEU
A
374
−7.024
78.314
24.787 
1.00
31.31


ATOM
2328
CD2
LEU
A
374
−4.706
78.910
25.584
1.00
33.89


ATOM
2329
N
CYS
A
375
−6.540
82.981 
24.574 
1.00
33.59


ATOM
2330
CA
CYS
A
375
−6.809
83.918 
25.669
1.00
34.34


ATOM
2331
C
CYS
A
375
−8.120
84.649
25.514
1.00
36.34


ATOM
2332
O
CYS
A
375
−8.862
84.801
26.470
1.00
35.60


ATOM
2333
CB
CYS
A
375
−5.664
84.912 
25.820
1.00
35.36


ATOM
2334
SG
CYS
A
375
−4.145
84.097
26.378
1.00
39.65


ATOM
2335
N
SER
A
376
−8.399
85.108
24.299 
1.00
31.43


ATOM
2336
CA
SER
A
376
−9.638
85.822 
24.032 
1.00
31.06


ATOM
2337
C
SER
A
376
−10.857
84.884
24.054 
1.00
34.85


ATOM
2338
O
SER
A
376
−11.958
85.286
24.427
1.00
33.78


ATOM
2339
CB
SER
A
376
−9.554
86.567
22.698 
1.00
33.39


ATOM
2340
OG
SER
A
376
−9.418
85.662
21.626 
1.00
44.30


ATOM
2341
N
THR
A
377
−10.634
83.627
23.678
1.00
30.94


ATOM
2342
CA
THR
A
377
−11.700
82.627
23.627 
1.00
30.21


ATOM
2343
C
THR
A
377
−12.142
82.136
25.013 
1.00
35.45


ATOM
2344
O
THR
A
377
−13.313
81.888
25.242
1.00
34.76


ATOM
2345
CB
THR
A
377
−11.245
81.385
22.857
1.00
35.17


ATOM
2346
OG1
THR
A
377
−11.231
81.670
21.464
1.00
29.13


ATOM
2347
CG2
THR
A
377
−12.176
80.206
23.132
1.00
36.31


ATOM
2348
N
ILE
A
378
−11.195
82.063
25.926
1.00
32.84


ATOM
2349
CA
ILE
A
378
−11.548
81.640
27.262
1.00
33.55


ATOM
2350
C
ILE
A
378
−11.541
82.791
28.258
1.00
38.76


ATOM
2351
O
ILE
A
378
−11.792
82.595
29.433
1.00
37.38


ATOM
2352
CB
ILE
A
378
−10.708
80.428
27.753
1.00
35.70


ATOM
2353
CG1
ILE
A
378
−9.244
80.823
27.951
1.00
35.60


ATOM
2354
CG2
ILE
A
378
−10.814
79.282
26.753
1.00
35.88


ATOM
2355
CD1
ILE
A
378
−8.447
79.818
28.799
1.00
38.76


ATOM
2356
N
GLY
A
379
−11.289
83.997
27.763
1.00
38.23


ATOM
2357
CA
GLY
A
379
−11.296
85.184
28.612
1.00
39.66


ATOM
2358
C
GLY
A
379
−10.172
85.106
29.628
1.00
48.17


ATOM
2359
O
GLY
A
379
−10.393
85.254
30.826
1.00
47.55


ATOM
2360
N
LEU
A
380
−8.963
84.846
29.141
1.00
48.58


ATOM
2361
CA
LEU
A
380
−7.805
84.726
30.005
1.00
50.34


ATOM
2362
C
LEU
A
380
−7.116
86.065
30.182
1.00
58.57


ATOM
2363
O
LEU
A
380
−6.733
86.722
29.210
1.00
58.74


ATOM
2364
CB
LEU
A
380
−6.826
83.695
29.447
1.00
50.50


ATOM
2365
CG
LEU
A
380
−6.444
82.585
30.429
1.00
55.14


ATOM
2366
CD1
LEU
A
380
−5.547
81.545
29.769
1.00
54.69


ATOM
2367
CD2
LEU
A
380
−5.771
83.190
31.654
1.00
58.66


ATOM
2368
N
ASN
A
381
−6.973
86.477
31.446
1.00
57.47


ATOM
2369
CA
ASN
A
381
−6.335
87.747
31.780
1.00
58.33


ATOM
2370
C
ASN
A
381
−5.003
87.522
32.478
1.00
64.77


ATOM
2371
O
ASN
A
381
−4.814
86.4.96 
33.145
1.00
64.63


ATOM
2372
CB
ASN
A
381
−7.248
88.577
32.682
1.00
59.09


ATOM
2373
CG
ASN
A
381
−8.452
89.114
31.949
1.00
81.90


ATOM
2374
CD1
ASN
A
381
−8.322
89.744
30.895
1.00
76.05


ATOM
2375
ND2
ASN
A
381
−9.640
88.826
32.473
1.00
72.34


ATOM
2376
N
GLN
A
382
−4.240
88.606
32.597
1.00
62.34


TER
2377

GLN
A
382







ATOM
2378
OW
WAT
W
1
−4.624
75.081
9.034
1.00
27.68


ATOM
2379
OW
WAT
W
2
−2.577
76.231
11.416
1.00
29.05


ATOM
2380
OW
WAT
W
3
−3.742
69.081
−1.006
1.00
30.37


ATOM
2381
OW
WAT
W
4
−14.964
74.471
13.770
1.00
31.93


ATOM
2382
OW
WAT
W
5
−11.919
57.539
7.244
1.00
31.88


ATOM
2383
OW
WAT
W
6
−11.116
72.975
0.157
1.00
34.55


ATOM
2384
OW
WAT
W
7
−13.659
59.717
7.931
1.00
29.70


ATOM
2385
OW
WAT
W
8
−15.768
70.359
1.074
1.00
37.39


ATOM
2386
OW
WAT
W
9
3.702
73.039
22.508
1.00
36.83


ATOM
2387
OW
WAT
W
10
−8.014
61.681
−0.933
1.00
39.30


ATOM
2388
OW
WAT
W
11
−11.273
56.557
25.382
1.00
38.77


ATOM
2389
OW
WAT
W
12
−5.122
56.773
22.513
1.00
34.68


ATOM
2390
OW
WAT
W
13
−11.739
64.136
26.992
1.00
37.17


ATOM
2391
OW
WAT
W
14
0.443
78.008
32.084
1.00
40.11


ATOM
2392
OW
WAT
W
15
−15.623
64.996
5.192
1.00
43.40


ATOM
2393
OW
WAT
W
16
2.238
53.070
26.823
1.00
57.67


ATOM
2394
OW
WAT
W
17
−13.635
55.899
19.258
1.00
37.89


ATOM
2395
OW
WAT
W
18
−4.575
74.107
0.759
1.00
37.31


ATOM
2396
OW
WAT
W
19
6.331
61.007
12.977
1.00
55.43


ATOM
2397
OW
WAT
W
20
−12.774
76.436
10.591
1.00
32.37


ATOM
2398
OW
WAT
W
21
−16.438
53.903
28.861
1.00
37.30


ATOM
2399
OW
WAT
W
22
−13.743
86.024
26.513
1.00
32.43


ATOM
2400
OW
WAT
W
23
−9.971
61.068
2.309
1.00
30.02


ATOM
2401
OW
WAT
W
24
0.848
81.061
19.815
1.00
43.98


ATOM
2402
OW
WAT
W
25
−14.485
67.474
24.615
1.00
37.16


ATOM
2403
OW
WAT
W
26
−15.104
69.736
25.760
1.00
30.79


ATOM
2404
OW
WAT
W
27
9.647
67.025
20.957
1.00
42.41


ATOM
2405
OW
WAT
W
28
−2.745
69.882
47.685
1.00
40.30


ATOM
2406
OW
WAT
W
29
5.706
56.554
11.512
1.00
45.72


ATOM
2407
OW
WAT
W
30
−7.561
54.142
20.853
1.00
33.21


ATOM
2408
OW
WAT
W
31
−13.489
64.239
6.990
1.00
35.53


ATOM
2409
OW
WAT
W
32
−2.256
56.573
28.890
1.00
51.35


ATOM
2410
OW
WAT
W
33
−12.567
75.838
7.931
1.00
35.03


ATOM
2411
OW
MAT
W
34
−1.230
72.376 
0.289
1.00
33.27


ATOM
2412
OW
MAT
W
35
−18.950
72.658
22.382
1.00
45.98


ATOM
2413
OW
MAT
W
36
−13.377
31.955 
19.898
1.00
36.43


ATOM
2414
OW
MAT
W
37
−12.793
52.525 
7.544
1.00
39.83


ATOM
2415
OW
MAT
W
38
0.083 
71.523
1.897
1.00
40.55


ATOM
2416
OW
MAT
W
39
−8.845
57.963 
24.752
1.00
34.15


ATOM
2417
OW
MAT
W
40
−7.698 
74.969 
0.939
1.00
39.78


ATOM
2418
OW
MAT
W
41
7.596 
71.335 
27.791
1.00
46.01


ATOM
2419
OW
MAT
W
42
0.606
52.047 
6.698
1.00
68.67


ATOM
2420
OW
MAT
W
43
−16.485
53.782 
13.115
1.00
38.71


ATOM
2421
OW
MAT
W
44.
5.553
73.417 
6.486 
1.00
41.45


ATOM
2422
OW
MAT
W
45
7.623
75.582
24.046
1.00
42.35


ATOM
2423
OW
MAT
W
46
−15.108 
63.029 
3.481 
1.00
37.31


ATOM
2424
OW
MAT
W
47
−18.182 
68.179 
22.755
1.00
41.92


ATOM
2425
OW
MAT
W
48
−1.567 
57.544
4.781
1.00
55.51


ATOM
2426
OW
MAT
W
49
5.270 
54.963
7.087
1.00
58.04


ATOM
2427
OW
MAT
W
50
−18.114 
70.616 
24.150
1.00
49.89


ATOM
2428
OW
MAT
W
51
9.645 
74.346 
24.716
1.00
38.07


ATOM
2429
OW
MAT
W
52
−2.407
49.867 
15.654
1.00
50.52


ATOM
2430
OW
MAT
W
53
−23.191 
78.787
12.861
1.00
53.87


ATOM
2431
OW
MAT
W
54
−16.398
66.547
1.241 
1.00
35.37


ATOM
2432
OW
MAT
W
55
−7.301
55.4.28
23.272
1.00
44.58


ATOM
2433
OW
MAT
W
56
−20.130
65.504
10.826
1.00
62.25


ATOM
2434
OW
MAT
W
57
−9.620
75.975
30.030
1.00 
44.26


ATOM
2435
OW
MAT
W
58
−1.101
64.720 
1.776 
1.00
36.60


ATOM
2436
OW
MAT
W
59
−14.826
83.968 
26.930
1.00
42.76


ATOM
2437
OW
MAT
W
60
5.708 
74.961 
21.589
1.00 
44.72


ATOM
2438
OW
MAT
W
61
−10.828
50.524
6.804
1.00
44.09


ATOM
2439
OW
MAT
W
62
−0.626
71.455
−2.363
1.00 
40.36


ATOM
2440
OW
MAT
W
63
3.044
75.866 
31.540
1.00
45.03


ATOM
2441
OW
MAT
W
64
−15.437
60.223
3.728
1.00
45.44


ATOM
2442
OW
MAT
W
55
8.940 
61.511 
42.174
1.00
59.50


ATOM
2443
OW
MAT
W
66
−16.614
63.941 
1.497 
1.00
49.11


ATOM
2444
OW
MAT
W
67
−19.852
61.372
10.416
1.00
48.85


ATOM
2445
OW
MAT
W
68
−15.672 
51.995
6.737
1.00
54.00


ATOM
2446
OW
MAT
W
69
−23.534
50.004
8.328
1.00
62.07


ATOM
2447
OW
MAT
W
70
7.642
62.190
8.434 
1.00
50.04


ATOM
2448
OW
MAT
W
71
−15.960
68.780
44.824
1.00
62.11


ATOM
2449
OW
MAT
W
501
−7.359
61.090
31.982
1.00
36.24


ATOM
2450
OW
MAT
W
502
−6.203
65.450
32.091
1.00
37.46


ATOM
2451
OW
MAT
W
503
−3.790
65.392
33.857
1.00
45.57


ATOM
2452
OW
MAT
W
504
−11.919
68.273
31.788
1.00
44.80


ATOM
2453
OW
WAT
W
505
−7.520
72.809
34.057
1.00
42.61


ATOM
2454
OW
WAT
W
901
−18.486
78.358
18.478
0.50
34.54


ATOM
2455
OW
WAT
W
902
−20.684
77.106
18.477
0.50
46.09


ATOM
2456
OW
WAT
W
903
−7.421
66.578
0.296
0.50
24.89


ATOM
2457
OW
WAT
W
904
−4.836
67.095
−0.600
0.50
20.53


ATOM
2458
C01
SCE
Z
1
0.248
60.985
33.956
1.00
38.12


ATOM
2459
C02
SOH
Z
1
1.117
60.767
32.881
1.00
35.30


ATOM
2460
C03
SCH
Z
1
1.973
61.759
32.424
1.00
36.46


ATOM
2461
C04
SCH
Z
1
1.924
63.030
32.990
1.00
37.97


ATOM
2462
C05
SCH
Z
1
1.037 
63.306
34.032
1.00
39.21


ATOM
2463
C06
SCH
Z
1
0.218
62.286 
34.520
1.00
39.40


ATOM
2464
N07
SCH
Z
1
−0.593
59.962
34.455
1.00
41.43


ATOM
2465
C08
SCH
Z
1
−0.807
58.612
34.081
1.00
44.00


ATOM
2466
C09
SCH
Z
1
−2.123
58.154
33.881
1.00
46.76


ATOM
2467
C10
SCH
Z
1
−2.402
56.826
33.502
1.00
41.31


ATOM
2468
C11
SCH
Z
1
−1.358
55.933
33.295
1.00
45.40


ATOM
2469
C12
SCH
Z
1
−0.055
56.376
33.485
1.00
47.54


ATOM
2470
C13
SCH
Z
1
0.221
57.688
33.873
1.00
46.85


ATOM
2471
C14
SCH
Z
1
−3.231
59.068
34.167
1.00
50.08


ATOM
2472
N15
SCH
Z
1
4.441
58.731
33.628
1.00
53.33


ATOM
2473
O16
SCH
Z
1
−3.021
60.031
34.898
1.00
50.32


ATOM
2474
O17
SCH
Z
1
−5.503
59.651
33.782
1.00
56.97


ATOM
2475
C18
SCH
Z
1
−5.768
99.848
35.183
1.00
60.39


ATOM
2476
C19
SCH
Z
1
−7.246
60.141
35.358
1.00 
62.23


ATOM
2477
C20
SCH
Z
1
−7.924
59.037
36.162
1.00
63.76


ATOM
2478
O21
SCH
Z
1
−7.880
60.195
34.068
1.00
62.27


ATOM
2479
O22
SCH
Z
1
−9.272
58.901
35.699
1.00
64.75


ATOM
2480
I23
SCH
Z
1
3.170
64.505
32.262
1.00
41.66


ATOM
2481
CL24
SCR
Z
1
−0.862
62.667
35.820
1.00
41.85


ATOM
2482
F25
SCH
Z
1
1.509
58.023
34.034
1.00
48.39


ATOM
2483
F26
SCR
Z
1
0.948
55.529
33.267
1.00
50.88


ATOM
2484
PG
AGS
Z
2
−10.915
60.811
32.987
1.00
63.04


ATOM
2485
S1G
AGS
Z
2
−12.339
60.025
32.561
1.00
70.14


ATOM
2486
O2G
AGS
Z
2
−9.797
60.430
32.041
1.00
61.31


ATOM
2487
O3G
AGS
Z
2
−10.513
60.504
34.506
1.00
63.60


ATOM
2488
PB
AGS
Z
2
−10.232
63.584
32.898
1.00
48.34


ATOM
2489
O1B
AGS
Z
2
−9.044
63.367
31.978
1.00
44.81


ATOM
2490
O2B
AGS
Z
2
−10.911
64.870
32.526
1.00
48.17


ATOM
2491
O3B
AGS
Z
2
−11.244
62.368
32.871
1.00
56.01


ATOM
2492
PA
AGS
Z
2
−6.349
63.982
35.069
1.00
45.11


ATOM
2493
O1A
AGS
Z
2
−8.225
63.477
36.481
1.00
48.51


ATOM
2494
O2A
AGS
Z
2
−7.222
63.411
34.292
1.00
45.50


ATOM
2495
O3A
AGS
Z
2
−9.769
63.706
34.438
1.00
48.80


ATOM
2496
O5*
AGS
Z
2
−8.184
65.547
35.048
1.00
41.41


ATOM
2497
C5*
AGS
Z
2
−9.234
66.395
35.556
1.00
41.72


ATOM
2498
C4*
AGS
Z
2
−9.043
67.753
34.875
1.00
42.34


ATOM
2499
O4*
AGS
Z
2
−7.892
68.468
35.433
1.00
40.38


ATOM
2500
C3*
AGS
Z
2
−8.720
67.679
33.390
1.00
43.20


ATOM
2501
O3*
AGS
Z
2
−9.925
67.477
32.654
1.00
46.68


ATOM
2502
C2*
AGS
Z
2
−7.934
68.981
33.146
1.00
41.16


ATOM
2503
O2*
AGS
Z
2
−8.804
70.028
32.765
1.00
45.58


ATOM
2504
C1*
AGS
Z
2
−7.320
69.361
34.514
1.00
39.19


ATOM
2505
N9
AGS
Z
2
−5.849
69.222
34.538
1.00
35.77


ATOM
2506
C8
AGS
Z
2
−5.110
68.063
34.574
1.00
34.60


ATOM
2507
N7
AGS
Z
2
−3.761
68.278
34.486
1.00
35.25


ATOM
2508
C5
AGS
Z
2
−3.615
69.666
34.394
1.00
32.84


ATOM
2509
C6
AGS
Z
2
−2.445
70.482
34.310
1.00
33.19


ATOM
2510
N6
AGS
Z
2
−1.220
70.154
34.258
1.00
33.65


ATOM
2511
N1
AGS
Z
2
−2.787
71.799
34.247
1.00
33.38


ATOM
2512
C2
AGS
Z
2
−4.074
72.328
34.226
1.00
34.07


ATOM
2513
N3
AGS
Z
2
−5.162
71.586
34.332
1.00
32.84


ATOM
2514
C4
AGS
Z
2
−4.900
70.261
34.414
1.00
32.95


TER
2515

AGS
Z
2







ATOM
2516
MC+2
MG
Z
3
−6.773
63.248
31.971
1.00
25.75


TER
2517

MG
Z
3







END
















TABLE 3





Structural Coordinate of MEK1/N35/NKFCdel (corresponding to amino acids


24-373 of SEQ ID NO: 2)-ATPγS Binary Complex.

























ATOM
1
N
GLU
A
38
11.237
65.467
13.135
1.00
88.80


ATOM
2
CA
GLU
A
38
10.153
66.289
13.663
1.00
88.50


ATOM
3
C
GLU
A
38
10.352
66.568
15.147
1.00
91.34


ATOM
4
O
GLU
A
38
9.598
67.330
15.751
1.00
90.72


ATOM
5
CB
GLU
A
39
8.795
65.612
13.426
1.00
89.84


ATOM
6
CG
GLU
A
38
8.798
64.106
13.639
1.00
99.63


ATOM
7
CD
GLU
A
38
9.084
63.332
12.362
1.00
118.09


ATOM
8
OE1
GLU
A
38
8.189
62.594
11.897
1.00
102.03


ATOM
9
OE2
GLU
A
38
10.210
63.447
11.835
1.00
113.34


ATOM
10
N
LEU
A
39
11.375
65.948
15.727
1.00
87.45


ATOM
11
CA
LEU
A
39
11.684
66.134
17.142
1.00
65.90


ATOM
12
C
LEU
A
39
12.767
67.198
17.352
1.00
90.27


ATOM
13
O
LEU
A
39
13.338
67.316
18.440
1.00
89.67


ATOM
14
CB
LEU
A
39
12.081
64.801
17.795
1.00
86.89


ATOM
15
CG
LEU
A
39
11.000
63.706
17.774
1.00
91.43


ATOM
16
CD1
LEU
A
39
11.347
62.545
18.699
1.00
91.37


ATOM
17
CD2
LEU
A
39
9.616
64.274
18.110
1.00
93.64


ATOM
18
N
GLU
A
40
13.029
67.978
16.305
1.00
86.64


ATOM
19
CA
GLU
A
40
14.006
69.061
16.377
1.00
86.37


ATOM
20
C
GLU
A
40
13.411
70.192
17.214
1.00
88.29


ATOM
21
O
GLU
A
40
12.214
70.481
17.118
1.00
88.25


ATOM
22
CB
GLU
A
40
14.347
69.570
14.973
1.00
87.97


ATOM
23
CG
GLU
A
40
15.477
68.815
14.287
1.00
100.54


ATOM
24
CD
GLU
A
40
15.553
69.109
12.796
1.00
125.63


ATOM
25
OE1
GLU
A
40
14.732
69.913
12.302
1.00
121.03


ATOM
26
OE2
GLU
A
40
16.439
68.543
12.120
1.00
121.70


ATOM
27
N
LEU
A
41
14.238
70.816
18.045
1.00
82.50


ATOM
28
CA
LEU
A
41
13.762
71.867
18.930
1.00
81.07


ATOM
29
C
LEU
A
41
14.057
73.282
18.453
1.00
82.46


ATOM
30
O
LEU
A
41
15.172
73.601
18.052
1.00
81.68


ATOM
31
CB
LEU
A
41
14.303
71.663
20.345
1.00
81.02


ATOM
32
CG
LEU
A
41
13.537
70.667
21.215
1.00
85.49


ATOM
33
CD1
LEU
A
41
13.163
71.298
22.545
1.00
85.57


ATOM
34
CD2
LEU
A
41
12.301
70.165
20.488
1.00
87.93


ATOM
35
N
ASP
A
42
13.045
74.133
18.530
1.00
77.53


ATOM
36
CA
ASP
A
42
13.195
75.526
18.169
1.00
76.52


ATOM
37
C
ASP
A
42
14.164
76.158
19.158
1.00
77.60


ATOM
38
O
ASP
A
42
14.590
75.514
20.119
1.00
76.66


ATOM
39
CB
ASP
A
42
11.841
76.235
18.262
1.00
78.54


ATOM
40
CG
ASP
A
42
11.741
77.415
17.330
1.00
90.83


ATOM
41
OD1
ASP
A
42
10.843
77.408
16.461
1.00
91.56


ATOM
42
OD2
ASP
A
42
12.570
78.346
17.455
1.00
97.95


ATOM
43
N
GLU
A
43
14.497
77.422
18.931
1.00
72.29


ATOM
44
CA
GLU
A
43
15.392
78.140
19.825
1.00
71.12


ATOM
45
C
GLU
A
43
14.636
78.539
21.091
1.00
71.37


ATOM
46
O
GLU
A
43
15.105
78.311
22.201
1.00
70.09


ATOM
47
CB
GLU
A
43
15.961
79.382
19.131
1.00
72.63


ATOM
48
CG
GLU
A
43
17.386
79.210
18.626
1.00
84.55


ATOM
49
CD
GLU
A
43
18.196
80.496
18.698
1.00
107.21


ATOM
50
OE1
GLU
A
43
17.639
81.532
19.128
1.00
105.33


ATOM
51
OE2
GLU
A
43
19.392
80.466
18.329
1.00
98.51


ATOM
52
N
GLN
A
44
13.452
79.112
20.907
1.00
66.25


ATOM
53
CA
GLN
A
44
12.617
79.523
22.025
1.00
65.54


ATOM
54
C
GLN
A
44
12.123
78.295
22.773
1.00
67.92


ATOM
55
O
GLN
A
44
11.885
78.339
23.980
1.00
67.38


ATOM
56
CB
GLN
A
44
11.428
80.347
21.530
1.00
66.93


ATOM
57
CG
GLN
A
44
10.224
80.298
22.446
1.00
81.44


ATOM
58
CD
GLN
A
44
8.986
80.900
21.813
1.00
97.65


ATOM
59
OE1
GLN
A
44
8.291
80.246
21.032
1.00
91.57


ATOM
60
NE2
GLN
A
44
8.697
82.153
22.154
1.00
88.69


ATOM
61
N
GLN
A
45
11.981
77.195
22.047
1.00
63.28


ATOM
62
CA
GLN
A
45
11.549
75.947
22.641
1.00
62.43


ATOM
63
C
GLN
A
45
12.651
75.417
23.545
1.00
66.05


ATOM
64
O
GLN
A
45
12.428
75.163
24.726
1.00
65.74


ATOM
65
CB
GLN
A
45
11.247
74.921
21.551
1.00
63.53


ATOM
66
CG
GLN
A
45
9.858
75.034
20.938
1.00
68.54


ATOM
67
CD
GLN
A
45
9.547
73.876
20.006
1.00
77.29


ATOM
68
OE1
GLN
A
45
10.444
73.319
19.369
1.00
68.67


ATOM
69
NE2
GLN
A
45
8.277
73.501
19.931
1.00
68.21


ATOM
70
N
ARG
A
46
13.842
75.252
22.973
1.00
62.19


ATOM
71
CA
ARG
A
46
15.000
74.736
23.702
1.00
61.63


ATOM
72
C
ARG
A
46
15.287
75.523
24.971
1.00
64.18


ATOM
73
O
ARG
A
46
15.647
74.952
25.999
1.00
63.67


ATOM
74
CB
ARG
A
46
16.241
74.732
22.803
1.00
61.97


ATOM
75
CG
ARG
A
46
17.281
73.708
23.206
1.00
74.65


ATOM
76
CD
ARG
A
46
18.658
74.341
23.387
1.00
87.34


ATOM
77
NE
ARG
A
46
19.030
74.478
24.795
1.00
95.70


ATOM
78
CZ
ARG
A
46
18.893
73.520
25.708
1.00
110.85


ATOM
79
NH1
ARG
A
46
18.383
72.340
25.374
1.00
97.35


ATOM
80
NH2
ARG
A
46
19.258
73.747
26.961
1.00
99.53


ATOM
81
N
LYS
A
47
15.143
76.837
24.888
1.00
60.06


ATOM
82
CA
LYS
A
47
15.380
77.699
26.031
1.00
59.74


ATOM
83
C
LYS
A
47
14.330
77.462
27.120
1.00
63.78


ATOM
84
O
LYS
A
47
14.642
77.486
28.309
1.00
63.75


ATOM
85
CB
LYS
A
47
15.392
79.169
25.597
1.00
61.94


ATOM
86
CG
LYS
A
47
14.563
80.090
26.471
1.00
74.94


ATOM
87
CD
LYS
A
47
13.696
81.024
25.627
1.00
84.73


ATOM
88
CE
LYS
A
47
14.527
81.775
24.590
1.00
94.02


ATOM
89
NZ
LYS
A
47
13.830
83.001
24.092
1.00
100.80


ATOM
90
N
ARG
A
48
13.091
77.216
26.704
1.00
60.11


ATOM
91
CA
ARG
A
48
12.000
76.965
27.642
1.00
59.81


ATOM
92
C
ARG
A
48
12.162
75.623
28.367
1.00
63.62


ATOM
93
O
ARG
A
48
11.817
75.493
29.548
1.00
63.26


ATOM
94
CB
ARG
A
48
10.656
77.020
26.925
1.00
59.80


ATOM
95
CG
ARG
A
48
10.069
78.420
26.807
1.00
69.22


ATOM
96
CD
ARG
A
48
8.668
78.382
26.233
1.00
78.57


ATOM
97
NE
ARG
A
48
8.219
79.698
25.795
1.00
89.53


ATOM
98
CZ
ARG
A
48
7.700
79.949
24.600
1.00
103.86


ATOM
99
NH1
ARG
A
48
7.566
78.971
23.717
1.00
91.94


ATOM
100
NH2
ARG
A
48
7.314
81.178
24.287
1.00
90.91


ATOM
101
N
LEU
A
49
12.693
74.633
27.659
1.00
59.61


ATOM
102
CA
LEU
A
49
12.922
73.313
28.235
1.00
59.26


ATOM
103
C
LEU
A
49
14.045
73.397
29.265
1.00
63.05


ATOM
104
O
LEU
A
49
13.983
72.787
30.334
1.00
62.63


ATOM
105
CB
LEU
A
49
13.307
72.324
27.136
1.00
59.37


ATOM
106
CG
LEU
A
49
12.740
70.911
27.252
1.00
64.42


ATOM
107
CD1
LEU
A
49
12.291
70.618
28.685
1.00
64.64


ATOM
108
CD2
LEU
A
49
11.600
70.703
26.267
1.00
66.64


ATOM
109
N
GLU
A
50
15.071
74.167
28.930
1.00
59.50


ATOM
110
CA
GLU
A
50
16.209
74.361
29.810
1.00
59.12


ATOM
111
C
GLU
A
50
15.745
75.005
31.113
1.00
60.51


ATOM
112
O
GLU
A
50
16.051
74.525
32.207
1.00
59.92


ATOM
113
CB
GLU
A
50
17.224
75.274
29.127
1.00
60.81


ATOM
114
CG
GLU
A
50
18.670
74.986
29.461
1.00
73.47


ATOM
115
CD
GLU
A
50
19.615
75.958
28.772
1.00
98.72


ATOM
116
OE1
GLU
A
50
19.683
75.933
27.524
1.00
85.73


ATOM
117
OE2
GLU
A
50
20.245
76.782
29.473
1.00
98.75


ATOM
118
N
ALA
A
51
14.993
76.093
30.980
1.00
55.29


ATOM
119
CA
ALA
A
51
14.481
76.836
32.132
1.00
54.03


ATOM
120
C
ALA
A
51
13.607
75.980
33.037
1.00
55.66


ATOM
121
O
ALA
A
51
13.629
76.139
34.254
1.00
56.01


ATOM
122
CB
ALA
A
51
13.722
78.070
31.675
1.00
54.47


ATOM
123
N
PHE
A
52
12.845
75.064
32.444
1.00
49.53


ATOM
124
CA
PHE
A
52
11.971
74.200
33.228
1.00
48.27


ATOM
125
C
PHE
A
52
12.740
73.206
34.088
1.00
52.84


ATOM
126
O
PHE
A
52
12.381
72.967
35.238
1.00
51.77


ATOM
127
CB
PHE
A
52
10.973
73.462
32.341
1.00
48.87


ATOM
128
CG
PHE
A
52
10.095
72.506
33.094
1.00
48.93


ATOM
129
CD1
PHE
A
52
8.998
72.968
33.813
1.00
50.24


ATOM
130
CD2
PHE
A
52
10.387
71.150
33.122
1.00
49.89


ATOM
131
CE1
PHE
A
52
8.192
72.099
34.506
1.00
50.42


ATOM
132
CE2
PEE
A
52
9.581
70.274
33.819
1.00
52.17


ATOM
133
CZ
SHE
A
52
8.482
70.752
34.515
1.00
49.93


ATOM
134
N
LEU
A
53
13.787
72.621
33.519
1.00
51.13


ATOM
135
CA
LEU
A
53
14.613
71.652
34.245
1.00
51.55


ATOM
136
C
LEU
A
53
15.409
72.341
35.337
1.00
56.39


ATOM
137
O
LEU
A
53
15.551
71.822
36.443
1.00
55.83


ATOM
138
CB
LEU
A
53
15.555
70.935
33.293
1.00
51.59


ATOM
139
CG
LEU
A
53
14.873
69.937
32.369
1.00
56.33


ATOM
140
CD1
LEU
A
53
15.615
69.839
31.048
1.00
56.35


ATOM
141
CD2
LEU
A
53
14.773
68.578
33.047
1.00
58.93


ATOM
142
N
THE
A
54
15.931
73.517
35.024
1.00
53.69


ATOM
143
CA
THR
A
54
16.682
74.280
36.004
1.00
53.92


ATOM
144
C
THR
A
54
15.802
74.492
37.235
1.00
58.73


ATOM
145
O
THE
A
54
16.241
74.287
38.364
1.00
58.82


ATOM
146
CB
THR
A
54
17.112
75.645
35.441
1.00
59.69


ATOM
147
OG1
THE
A
54
17.787
75.456
34.191
1.00
57.99


ATOM
148
OG2
THR
A
54
18.038
76.353
36.409
1.00
56.90


ATOM
149
N
GLN
A
55
14.545
74.874
37.006
1.00
54.94


ATOM
150
CA
GLN
A
55
13.607
75.084
38.105
1.00
54.44


ATOM
151
C
GLN
A
55
13.343
73.770
38.845
1.00
57.83


ATOM
152
O
GLN
A
55
13.507
73.693
40.057
1.00
57.68


ATOM
153
CB
GLN
A
55
12.293
75.691
37.601
1.00
55.66


ATOM
154
CG
GLN
A
55
12.446
77.052
36.934
1.00
75.41


ATOM
155
CD
GLN
A
55
11.102
77.705
36.610
1.00
103.98


ATOM
156
OE1
GLN
A
55
10.259
77.119
35.919
1.00
100.16


ATOM
157
NE2
GLN
A
55
10.902
78.926
37.102
1.00
98.92


ATOM
158
N
LYS
A
56
12.968
72.734
38.100
1.00
54.03


ATOM
159
CA
LYS
A
56
12.698
71.417
38.682
1.00
53.55


ATOM
160
C
LYS
A
56
13.930
70.882
39.410
1.00
58.27


ATOM
161
O
LYS
A
56
13.845
69.944
40.198
1.00
58.33


ATOM
162
CB
LYS
A
56
12.261
70.436
37.593
1.00
55.32


ATOM
163
CG
LYS
A
56
12.617
68.992
37.873
1.00
62.95


ATOM
164
CD
LYS
A
56
11.509
68.057
37.409
1.00
69.51


ATOM
165
CE
LYS
A
56
12.006
66.630
37.246
1.00
74.10


ATOM
166
NZ
LYS
A
56
11.270
65.920
36.165
1.00
81.95


ATOM
167
N
GLN
A
57
15.075
71.492
39.141
1.00
55.10


ATOM
168
CA
GLN
A
57
16.325
71.095
39.768
1.00
55.03


ATOM
169
C
GLN
A
57
16.381
71.633
41.204
1.00
58.20


ATOM
170
O
GLN
A
57
16.800
70.935
42.118
1.00
57.42


ATOM
171
CB
GLN
A
57
17.512
71.625
38.957
1.00
56.61


ATOM
172
CG
GLN
A
57
18.578
70.583
38.644
1.00
76.82


ATOM
173
CD
GLN
A
57
18.039
69.416
37.830
1.00
100.63


ATOM
174
OE1
GLN
A
57
18.721
68.406
37.646
1.00
98.78


ATOM
175
NE2
GLN
A
57
16.815
69.557
37.331
1.00
91.54


ATOM
176
N
LYS
A
58
15.931
72.875
41.383
1.00
54.27


ATOM
177
CA
LYS
A
58
15.911
73.514
42.689
1.00
53.89


ATOM
178
C
LYS
A
58
14.938
72.846
43.663
1.00
58.58


ATOM
179
O
LYS
A
58
15.126
72.887
44.881
1.00
57.85


ATOM
180
CB
LYS
A
58
15.564
74.996
42.550
1.00
55.86


ATOM
181
CG
LYS
A
58
16.534
75.779
41.665
1.00
62.70


ATOM
182
CD
LYS
A
58
15.985
77.169
41.328
1.00
69.03


ATOM
183
CE
LYS
A
58
16.979
77.956
40.482
1.00
78.12


ATOM
184
NZ
LYS
A
58
16.988
79.418
40.810
1.00
82.80


ATOM
185
N
VAL
A
59
13.893
72.225
43.120
1.00
56.06


ATOM
186
CA
VAL
A
59
12.903
71.536
43.945
1.00
55.92


ATOM
187
C
VAL
A
59
13.513
70.233
44.436
1.00
60.13


ATOM
188
O
VAL
A
59
14.315
69.606
43.735
1.00
60.35


ATOM
189
CB
VAL
A
59
11.601
71.244
43.141
1.00
59.87


ATOM
190
CG1
VAL
A
59
10.486
70.790
44.076
1.00
59.65


ATOM
191
CG2
VAL
A
59
11.161
72.466
42.356
1.00
59.81


ATOM
192
N
GLY
A
60
13.180
69.844
45.651
1.00
56.15


ATOM
193
CA
GLY
A
60
13.733
68.617
46.200
1.00
56.20


ATOM
194
C
GLY
A
60
12.704
67.516
46.114
1.00
61.18


ATOM
195
O
GLY
A
60
11.966
67.421
45.130
1.00
61.14


ATOM
196
N
GLU
A
61
12.653
66.684
47.146
1.00
57.92


ATOM
197
CA
GLU
A
61
11.674
65.621
47.209
1.00
57.86


ATOM
198
C
GLU
A
61
10.334
66.258
47.554
1.00
60.64


ATOM
199
O
GLU
A
61
10.268
67.159
48.393
1.00
60.53


ATOM
200
CB
GLU
A
61
12.068
64.600
48.276
1.00
59.42


ATOM
201
CG
GLU
A
61
11.671
63.177
47.937
1.00
73.65


ATOM
202
CD
GLU
A
61
12.746
62.442
47.156
1.00
99.64


ATOM
203
OE1
GLU
A
61
13.507
63.107
46.419
1.00
98.16


ATOM
204
OE2
GLU
A
61
12.824
61.197
47.271
1.00
93.51


ATOM
205
N
LEU
A
62
9.277
65.829
46.875
1.00
55.82


ATOM
206
CA
LEU
A
62
7.956
66.399
47.101
1.00
54.82


ATOM
207
C
LEU
A
62
7.301
65.808
48.335
1.00
57.10


ATOM
208
O
LEU
A
62
7.297
64.599
48.525
1.00
56.48


ATOM
209
CB
LEU
A
62
7.071
66.225
45.865
1.00
54.75


ATOM
210
CG
LEU
A
62
7.609
66.895
44.591
1.00
59.05


ATOM
211
CD1
LEU
A
62
6.618
66.791
43.434
1.00
58.82


ATOM
212
CD2
LEU
A
62
7.982
68.345
44.856
1.00
60.69


ATOM
213
N
LYS
A
63
6.769
66.676
49.186
1.00
53.03


ATOM
214
CA
LYS
A
63
6.131
66.241
50.429
1.00
52.36


ATOM
215
C
LYS
A
63
4.740
66.840
50.563
1.00
54.26


ATOM
216
O
LYS
A
63
4.527
68.011
50.252
1.00
53.53


ATOM
217
CB
LYS
A
63
6.993
66.631
51.637
1.00
54.84


ATOM
218
CG
LYS
A
63
8.372
65.988
51.645
1.00
69.91


ATOM
219
CD
LYS
A
63
8.879
65.773
53.060
1.00
81.08


ATOM
220
CE
LYS
A
63
9.316
64.328
53.279
1.00
90.79


ATOM
221
NZ
LYS
A
63
9.676
64.063
54.702
1.00
99.66


ATOM
222
N
ASP
A
64
3.798
66.026
51.023
1.00
49.71


ATOM
223
CA
ASP
A
64
2.412
66.452
51.182
1.00
49.37


ATOM
224
C
ASP
A
64
2.270
67.803
51.873
1.00
52.19


ATOM
225
O
ASP
A
64
1.710
68.747
51.306
1.00
51.16


ATOM
226
CB
ASP
A
64
1.612
65.399
51.955
1.00
51.28


ATOM
227
CG
ASP
A
64
0.202
65.856
52.275
1.00
63.90


ATOM
228
OD1
ASP
A
64
−0.593
66.043
51.333
1.00
65.29


ATOM
229
OD2
ASP
A
64
−0.110
66.036
53.470
1.00
72.24


ATOM
230
N
ASP
A
65
2.747
67.874
53.112
1.00
47.78


ATOM
231
CA
ASP
A
65
2.618
69.080
53.914
1.00
47.13


ATOM
232
C
ASP
A
65
3.279
70.330
53.286
1.00
49.75


ATOM
233
O
ASP
A
65
3.039
71.447
53.736
1.00
49.05


ATOM
234
CB
ASP
A
65
3.115
68.839
55.360
1.00
49.26


ATOM
235
CG
ASP
A
65
2.266
67.788
56.132
1.00
61.44


ATOM
236
OD1
ASP
A
65
1.380
67.133
55.519
1.00
61.23


ATOM
237
OD2
ASP
A
65
2.503
67.615
57.359
1.00
71.25


ATOM
238
N
ASP
A
66
4.067
70.142
52.227
1.00
45.54


ATOM
239
CA
ASP
A
66
4.725
71.273
51.557
1.00
45.21


ATOM
240
C
ASP
A
66
3.827
71.940
50.512
1.00
49.34


ATOM
241
O
ASP
A
66
4.234
72.898
49.842
1.00
48.47


ATOM
242
CB
ASP
A
66
6.026
70.827
50.897
1.00
47.47


ATOM
243
CG
ASP
A
66
7.141
70.581
51.903
1.00
59.55


ATOM
244
OD1
ASP
A
66
7.179
71.281
52.939
1.00
60.26


ATOM
245
OD2
ASP
A
66
7.986
69.696
51.650
1.00
65.13


ATOM
246
N
PHE
A
67
2.609
71.425
50.368
1.00
45.66


ATOM
247
CA
PHE
A
67
1.674
71.939
49.379
1.00
44.35


ATOM
248
C
PHE
A
67
0.535
72.733
49.982
1.00
47.94


ATOM
249
O
PEE
A
67
0.089
72.463
51.090
1.00
46.77


ATOM
250
CB
PHE
A
67
1.135
70.800
48.507
1.00
45.26


ATOM
251
CG
PHE
A
67
2.136
70.275
47.527
1.00
45.79


ATOM
252
CD1
PHE
A
67
2.339
70.912
45.319
1.00
47.94


ATOM
253
CD2
PHE
A
67
2.915
69.182
47.838
1.00
47.15


ATOM
254
CE1
PHE
A
67
3.287
70.454
45.438
1.00
48.53


ATOM
255
CE2
PHE
A
67
3.870
68.727
46.962
1.00
49.59


ATOM
256
CZ
PHE
A
67
4.055
69.358
45.763
1.00
47.60


ATOM
257
N
GLU
A
68
0.066
73.713
49.224
1.00
45.69


ATOM
258
CA
GLU
A
68
−1.029
74.571
49.633
1.00
45.71


ATOM
259
C
GLU
A
68
−1.990
74.688
46.437
1.00
49.76


ATOM
260
O
GLU
A
68
−1.589
75.109
47.347
1.00
49.04


ATOM
261
CB
GLU
A
68
−0.477
75.949
50.023
1.00
47.07


ATOM
262
CG
GLU
A
68
−1.509
76.942
50.511
1.00
59.43


ATOM
263
CD
GLU
A
68
−1.021
78.383
50.400
1.00
88.13


ATOM
264
OE1
GLU
A
68
0.213
78.605
50.426
1.00
76.75


ATOM
265
OE2
GLU
A
68
−1.870
79.291
50.266
1.00
89.20


ATOM
266
N
LYS
A
69
−3.237
74.261
48.631
1.00
46.48


ATOM
267
CA
LYS
A
69
−4.230
74.287
47.563
1.00
46.99


ATOM
268
C
LYS
A
69
−4.671
75.702
47.192
1.00
52.61


ATOM
269
O
LYS
A
69
−4.935
76.537
48.062
1.00
52.73


ATOM
270
CB
LYS
A
69
−5.445
73.435
47.932
1.00
49.46


ATOM
271
CG
LYS
A
69
−6.579
73.526
46.930
1.00
65.02


ATOM
272
CD
LYS
A
69
−7.746
72.633
47.335
1.00
74.94


ATOM
273
CE
LYS
A
69
−9.066
73.146
46.767
1.00
82.52


ATOM
274
NZ
LYS
A
69
−10.221
72.301
47.193
1.00
88.63


ATOM
275
N
ILE
A
70
−4.740
75.967
45.893
1.00
49.32


ATOM
276
CA
ILE
A
70
−5.151
77.274
45.402
1.00
49.03


ATOM
277
C
ILE
A
70
−6.572
77.195
44.880
1.00
54.06


ATOM
278
O
ILE
A
70
−7.437
77.955
45.296
1.00
54.85


ATOM
279
CB
ILE
A
70
−4.245
77.763
44.263
1.00
51.81


ATOM
280
CG1
ILE
A
70
−2.809
77.933
44.752
1.00
51.56


ATOM
281
CG2
ILE
A
70
−4 .775
79.068
43.687
1.00
52.99


ATOM
282
CD1
ILE
A
70
−1.910
78.612
43.752
1.00
52.79


ATOM
283
N
SER
A
71
−6.809
76.261
43.975
1.00
50.28


ATOM
284
CA
SER
A
71
−8.128
76.076
43.406
1.00
50.24


ATOM
285
C
SER
A
71
−8.232
74.710
42.764
1.00
55.45


ATOM
286
O
SER
A
71
−7.242
73.977
42.666
1.00
55.08


ATOM
287
CB
SER
A
71
−8.419
77.160
42.367
1.00
53.17


ATOM
288
OG
SER
A
71
−7.354
77.271
41.432
1.00
60.02


ATOM
289
N
GLU
A
72
−9.433
74.370
42.323
1.00
53.13


ATOM
290
CA
GLU
A
73
−9.678
73.095
41.669
1.00
53.62


ATOM
291
C
GLU
A
72
−9.562
73.277
40.164
1.00
57.70


ATOM
292
O
GLU
A
72
−10.178
74.171
39.598
1.00
57.44


ATOM
293
CB
GLU
A
72
−11.066
72.570
42.034
1.00
55.21


ATOM
294
OG
GLU
A
72
−11.055
71.190
42.670
1.00
68.51


ATOM
295
CD
GLU
A
72
−12.091
71.045
43.775
1.00
90.12


ATOM
296
OE1
GLU
A
72
−12.607
72.079
44.250
1.00
82.31


ATOM
297
OE2
GLU
A
72
−12.385
69.897
44.170
1.00
85.74


ATOM
298
N
LEU
A
73
−8.746
72.442
39.526
1.00
54.70


ATOM
299
CA
LEU
A
73
−8.518
73.531
38.080
1.00
54.63


ATOM
300
C
LEU
A
73
−9.501
71.699
37.276
1.00
60.43


ATOM
301
O
LEU
A
73
−9.829
72.036
36.146
1.00
60.50


ATOM
302
CB
LEU
A
73
−7.096
72.101
37.737
1.00
54.38


ATOM
303
CG
LEU
A
73
−5.982
73.060
38.142
1.00
58.31


ATOM
304
CD1
LEU
A
73
−4.632
72.469
37.794
1.00
58.13


ATOM
305
CD2
LEU
A
73
−6.178
74.400
37.474
1.00
59.76


ATOM
306
N
GLY
A
74
−9.943
70.594
37.847
1.00
58.51


ATOM
307
CA
GLY
A
74
−10.869
69.717
37.162
1.00
59.58


ATOM
308
C
GLY
A
74
−10.870
68.355
37.822
1.00
66.53


ATOM
309
O
GLY
A
74
−10.102
68.107
38.756
1.00
66.15


ATOM
310
N
ALA
A
75
−11.729
67.466
37.334
1.00
65.14


ATOM
311
CA
ALA
A
75
−11.828
66.134
37.905
1.00
66.06


ATOM
312
C
ALA
A
75
−12.073
65.057
36.862
1.00
71.96


ATOM
313
O
ALA
A
75
−12.410
65.348
35.710
1.00
71.94


ATOM
314
CB
ALA
A
75
−12.911
66.097
38.973
1.00
66.81


ATOM
315
N
GLY
A
76
−11.909
63.808
37.281
1.00
69.54


ATOM
316
CA
GLY
A
76
−12.124
62.663
36.418
1.00
69.93


ATOM
317
C
GLY
A
76
−12.929
61.628
37.185
1.00
75.90


ATOM
318
O
GLY
A
76
−13.450
61.916
38.265
1.00
75.72


ATOM
319
N
ASN
A
77
−13.015
50.419
36.637
1.00
73.74


ATOM
320
CA
ASN
A
77
−13.777
59.333
37.257
1.00
74.06


ATOM
321
C
ASN
A
77
−13.037
58.643
38.417
1.00
78.60


ATOM
322
O
ASN
A
77
−13.129
57.417
38.593
1.00
78.46


ATOM
323
CB
ASN
A
77
−14.193
58.301
36.200
1.00
75.16


ATOM
324
CG
ASN
A
77
−14.768
58.945
34.947
1.00
101.10


ATOM
325
OD1
ASN
A
77
−15.445
59.976
35.016
1.00
95.52


ATOM
326
NO2
ASN
A
77
−14.505
58.335
33.794
1.00
92.98


ATOM
327
N
CLY
A
78
−12.331
59.430
39.221
1.00
74.93


ATOM
328
CA
CLY
A
78
−11.597
58.890
40.374
1.00
74.33


ATOM
329
C
GLY
A
78
−10.198
59.488
40.456
1.00
76.46


ATOM
330
O
GLY
A
78
−9.208
58.765
40.481
1.00
76.65


ATOM
331
N
GLY
A
79
−10.132
60.814
40.426
1.00
70.79


ATOM
332
CA
GLY
A
79
−8.860
61.526
40.479
1.00
69.29


ATOM
333
C
GLY
A
79
−9.098
63.021
40.247
1.00
69.97


ATOM
334
O
GLY
A
79
−9.444
63.456
39.143
1.00
69.20


ATOM
335
N
VAL
A
80
−8.943
63.794
41.311
1.00
63.87


ATOM
336
CA
VAL
A
80
−9.142
65.225
41.242
1.00
62.08


ATOM
337
C
VAL
A
80
−7.809
65.910
40.994
1.00
60.29


ATOM
338
O
VAL
A
80
−6.752
65.364
41.318
1.00
59.54


ATOM
339
CB
VAL
A
80
−9.754
65.753
42.545
1.00
66.76


ATOM
340
CG1
VAL
A
80
−10.386
67.136
42.327
1.00
66.69


ATOM
341
CG2
VAL
A
80
−10.789
64.756
43.082
1.00
66.70


ATOM
342
N
VAL
A
81
−7.859
67.092
40.387
1.00
52.52


ATOM
343
CA
VAL
A
81
−6.648
67.845
40.110
1.00
50.30


ATOM
344
C
VAL
A
81
−6.765
69.257
40.630
1.00
50.58


ATOM
345
O
VAL
A
81
−7.680
69.996
40.269
1.00
49.16


ATOM
346
CB
VAL
A
81
−6.281
67.853
38.603
1.00
53.36


ATOM
347
CG1
VAL
A
81
−4.956
68.587
38.385
1.00
52.57


ATOM
348
CG2
VAL
A
81
−6.197
66.433
38.071
1.00
53.11


ATOM
349
N
PHE
A
82
−5.836
69.624
41.496
1.00
46.26


ATOM
350
CA
PHE
A
82
−5.833
70.940
42.108
1.00
45.77


ATOM
351
C
PHE
A
82
−4.686
71.807
41.610
1.00
47.34


ATOM
352
O
PHE
A
82
−3.616
71.310
41.265
1.00
46.04


ATOM
353
CB
PHE
A
82
−5.720
70.803
43.631
1.00
47.78


ATOM
354
CG
PHE
A
82
−6.940
70.224
44.282
1.00
50.11


ATOM
355
CD1
PHE
A
82
−7.035
68.868
44.516
1.00
54.28


ATOM
356
CD2
PHE
A
82
−7.974
71.048
44.707
1.00
52.92


ATOM
357
CE1
PHE
A
82
−8.157
68.331
45.144
1.00
55.80


ATOM
358
CE2
PEE
A
82
−9.097
70.521
45.321
1.00
56.08


ATOM
359
CZ
PHE
A
82
−9.188
69.163
45.543
1.00
54.46


ATOM
360
N
LYS
A
83
−4.898
73.113
41.622
1.00
43.39


ATOM
361
CA
LYS
A
83
−3.831
74.044
41.301
1.00
42.61


ATOM
362
C
LYS
A
83
−3.225
74.362
42.654
1.00
44.84


ATOM
363
O
LYS
A
83
−3.941
74.724
43.585
1.00
44.32


ATOM
364
CB
LYS
A
83
−4.380
75.312
40.655
1.00
44.70


ATOM
365
CG
LYS
A
83
−3.311
76.227
40.111
1.00
51.78


ATOM
366
CD
LYS
A
83
−3.796
77.655
40.066
1.00
60.17


ATOM
367
CE
LYS
A
83
−2.689
78.594
39.632
1.00
70.37


ATOM
368
NZ
LYS
A
93
−3.236
79.882
39.118
1.00
82.16


ATOM
369
N
VAL
A
84
−1.930
74.131
42.796
1.00
40.24


ATOM
370
CA
VAL
A
84
−1.296
74.310
44.080
1.00
39.48


ATOM
371
C
VAL
A
84
−0.044
75.149
44.052
1.00
43.70


ATOM
372
O
VAL
A
84
0.552
75.411
42.995
1.00
42.77


ATOM
373
CB
VAL
A
84
−0.918
72.949
44.722
1.00
42.87


ATOM
374
CG1
VAL
A
64
−2.148
72.073
44.917
1.00
42.61


ATOM
375
CG2
VAL
A
84
0.145
72.237
43.887
1.00
42.42


ATOM
376
N
SER
A
85
0.382
75.512
45.251
1.00
40.39


ATOM
377
CA
SFR
A
85
1.597
76.237
45.458
1.00
40.07


ATOM
378
C
SER
A
85
2.531
75.318
46.247
1.00
44.37


ATOM
379
O
SER
A
85
2.147
74.776
47.290
1.00
43.07


ATOM
380
CB
SER
A
85
1.310
77.496
46.275
1.00
42.88


ATOM
381
OG
SER
A
85
2.501
78.034
46.805
1.00
51.75


ATOM
382
N
HIS
A
86
3.727
75.087
45.721
1.00
42.51


ATOM
383
CA
HIS
A
86
4.716
74.312
46.448
1.00
43.33


ATOM
384
C
HIS
A
86
5.455
75.331
47.317
1.00
48.17


ATOM
385
O
HIS
A
86
6.368
76.021
46.844
1.00
47.35


ATOM
386
CB
HIS
A
86
5.697
73.626
45.508
1.00
44.29


ATOM
387
CG
HIS
A
86
6.683
72.754
46.216
1.00
47.68


ATOM
388
ND1
HIS
A
86
8.038
73.005
46.212
1.00
49.52


ATOM
389
CD2
HIS
A
86
6.504
71.666
47.002
1.00
49.21


ATOM
390
CE1
HIS
A
86
8.654
72.095
46.947
1.00
48.74


ATOM
391
NE2
HIS
A
86
7.745
71.274
47.440
1.00
49.01


ATOM
392
N
LYS
A
87
4.978
75.481
48.552
1.00
45.01


ATOM
393
CA
LYS
A
87
5.484
76.475
49.502
1.00
44.81


ATOM
394
C
LYS
A
87
6.976
76.790
49.445
1.00
49.01


ATOM
395
O
LYS
A
87
7.369
77.923
49.154
1.00
49.57


ATOM
396
CB
LYS
A
87
5.060
76.125
50.932
1.00
46.85


ATOM
397
CG
LYS
A
87
3.595
76.427
51.233
1.00
55.27


ATOM
398
CD
LYS
A
87
2.815
75.154
51.499
1.00
63.63


ATOM
399
CE
LYS
A
87
2.036
75.245
52.799
1.00
73.12


ATOM
400
NZ
LYS
A
87
2.709
74.497
53.902
1.00
80.83


ATOM
401
N
PRO
A
88
7.803
75.797
49.733
1.00
44.97


ATOM
402
CA
PRO
A
88
9.255
75.994
49.767
1.00
44.58


ATOM
403
C
PRO
A
88
9.821
76.665
48.510
1.00
49.49


ATOM
404
O
PRO
A
88
10.459
77.721
48.586
1.00
49.49


ATOM
405
CB
PRO
A
88
9.801
74.565
49.912
1.00
45.80


ATOM
406
CG
PRO
A
88
8.628
73.751
50.382
1.00
49.93


ATOM
407
CD
PRO
A
88
7.448
74.374
49.725
1.00
45.20


ATOM
408
N
SER
A
89
9.593
76.040
47.362
1.00
46.13


ATOM
409
CA
SER
A
89
10.096
76.543
46.090
1.00
45.61


ATOM
410
C
SER
A
89
9.346
77.771
45.587
1.00
48.69


ATOM
411
O
SER
A
89
9.880
78.543
44.808
1.00
48.38


ATOM
412
CB
SER
A
89
10.023
75.440
45.034
1.00
49.15


ATOM
413
OG
SER
A
89
8.672
75.137
44.725
1.00
56.83


ATOM
414
N
GLY
A
90
8.097
77.931
46.009
1.00
45.19


ATOM
415
CA
GLY
A
90
7.269
79.039
45.532
1.00
44.77


ATOM
416
C
GLY
A
90
6.643
78.689
44.161
1.00
48.28


ATOM
417
O
GLY
A
90
5.863
79.468
43.595
1.00
47.35


ATOM
418
N
LEU
A
91
6.996
77.519
43.637
1.00
45.24


ATOM
419
CA
LEU
A
91
6.466
77.059
42.343
1.00
44.99


ATOM
420
C
LEU
A
91
4.987
76.706
42.440
1.00
47.71


ATOM
421
O
LEU
A
91
4.547
76.081
43.405
1.00
46.57


ATOM
422
CB
LEU
A
91
7.220
75.815
41.864
1.00
45.10


ATOM
423
CG
LEU
A
91
8.627
75.939
41.267
1.00
50.01


ATOM
424
CD1
LEU
A
91
8.896
74.750
40.370
1.00
50.15


ATOM
425
CD2
LEU
A
91
8.822
77.248
40.503
1.00
51.82


ATOM
426
N
VAL
A
92
4.236
77.082
41.416
1.00
44.23


ATOM
427
CA
VAL
A
92
2.834
76.718
41.312
1.00
43.81


ATOM
428
C
VAL
A
92
2.795
75.479
40.410
1.00
46.11


ATOM
429
O
VAL
A
92
3.566
75.381
39.459
1.00
46.12


ATOM
430
CB
VAL
A
92
2.008
77.836
40.661
1.00
47.91


ATOM
431
CG1
VAL
A
92
0.633
77.333
40.285
1.00
47.81


ATOM
432
CG2
VAL
A
92
1.899
79.021
41.595
1.00
47.79


ATOM
433
N
MET
A
93
1.967
74.505
40.762
1.00
40.56


ATOM
434
CA
MET
A
93
1.873
73.280
39.987
1.00
38.99


ATOM
435
C
MET
A
93
0.453
72.790
39.918
1.00
41.70


ATOM
436
O
MET
A
93
−0.444
73.305
40.604
1.00
40.92


ATOM
437
CB
MET
A
93
2.719
72.161
40.628
1.00
41.02


ATOM
438
CG
MET
A
93
3.999
72.613
41.219
1.00
44.12


ATOM
439
SD
MET
A
93
4.926
71.198
42.014
1.00
47.80


ATOM
440
CE
MET
A
93
6.622
71.800
41.863
1.00
44.47


ATOM
441
N
ALA
A
94
0.271
71.728
39.148
1.00
37.64


ATOM
442
CA
ALA
A
94
−0.996
71.036
39.073
1.00
37.27


ATOM
443
C
ALA
A
94
−0.746
69.748
39.825
1.00
40.99


ATOM
444
O
ALA
A
94
0.256
69.079
39.600
1.00
40.04


ATOM
445
CB
ALA
A
94
−1.360
70.747
37.624
1.00
38.04


ATOM
446
N
ARG
A
95
−1.601
69.446
40.784
1.00
38.81


ATOM
447
CA
ARG
A
95
−1.422
68.252
41.594
1.00
38.80


ATOM
448
C
ARG
A
95
−2.567
67.287
41.372
1.00
43.55


ATOM
449
O
ARG
A
95
−3.715
67.597
41.680
1.00
43.26


ATOM
450
CB
ARG
A
95
−1.325
68.629
43.085
1.00
37.43


ATOM
451
CG
ARG
A
95
−1.010
67.453
44.050
1.00
40.99


ATOM
452
CD
ARG
A
95
−1.032
67.933
45.524
1.00
43.19


ATOM
453
NE
ARG
A
95
−0.801
66.845
46.489
1.00
46.69


ATOM
454
CZ
ARG
A
95
−0.922
66.976
47.815
1.00
59.60


ATOM
455
NH1
ARG
A
95
−1.294
68.133
48.345
1.00
43.11


ATOM
456
NH2
ARG
A
95
−0.693
65.940
48.614
1.00
49.01


ATOM
457
N
LYS
A
96
−2.255
66.119
40.831
1.00
41.36


ATOM
458
CA
LYS
A
96
−3.274
65.092
40.624
1.00
42.12


ATOM
459
C
LYS
A
96
−3.279
64.137
41.807
1.00
47.52


ATOM
460
O
LYS
A
96
−2.236
63.603
42.199
1.00
46.28


ATOM
461
CB
LYS
A
96
−3.040
64.327
39.323
1.00
44.23


ATOM
462
CG
LYS
A
96
−4.221
63.453
38.894
1.00
54.01


ATOM
463
CD
LYS
A
96
−3.991
62.869
37.500
1.00
59.57


ATOM
464
CE
LYS
A
96
−5.287
62.680
36.751
1.00
60.81


ATOM
465
NZ
LYS
A
96
−5.098
61.851
35.539
1.00
63.49


ATOM
466
N
LEU
A
97
−4.449
63.955
42.400
1.00
46.66


ATOM
467
CA
LEU
A
97
−4.578
63.079
43.550
1.00
47.96


ATOM
468
C
LEU
A
97
−5.430
61.874
43.228
1.00
55.33


ATOM
469
O
LEU
A
97
−6.615
62.001
42.926
1.00
54.75


ATOM
470
CB
LEU
A
97
−5.164
63.837
44.743
1.00
48.01


ATOM
471
CG
LEU
A
97
−4.385
65.083
45.170
1.00
53.09


ATOM
472
CD1
LEU
A
97
−5.315
66.284
45.339
1.00
53.13


ATOM
473
CD2
LEU
A
97
−3.610
64.808
46.453
1.00
55.88


ATOM
474
N
ILE
A
98
−4.818
60.701
43.283
1.00
55.10


ATOM
475
CA
ILE
A
98
−5.534
59.461
43.037
1.00
56.46


ATOM
476
C
ILE
A
98
−5.673
58.721
44.356
1.00
64.11


ATOM
477
O
ILE
A
98
−4.678
58.288
44.935
1.00
63.09


ATOM
478
CB
ILE
A
98
−4.783
58.554
42.047
1.00
59.35


ATOM
479
CG1
ILE
A
98
−4.525
59.286
40.731
1.00
59.59


ATOM
480
CG2
ILE
A
98
−5.565
57.282
41.798
1.00
60.00


ATOM
481
CD1
ILE
A
98
−3.289
58.797
40.000
1.00
65.00


ATOM
482
N
HIS
A
99
−6.900
58.608
44.853
1.00
64.29


ATOM
483
CA
HIS
A
99
−7.117
57.894
46.096
1.00
66.09


ATOM
484
C
HIS
A
99
−7.155
56.405
45.853
1.00
71.91


ATOM
485
O
HIS
A
99
−8.038
55.897
45.148
1.00
71.49


ATOM
486
CB
HIS
A
99
−8.396
58.331
46.807
1.00
67.40


ATOM
487
CG
HIS
A
99
−8.505
57.805
48.207
1.00
71.33


ATOM
488
ND1
HIS
A
99
−8.256
58.587
49.317
1.00
73.33


ATOM
489
CD2
HIS
A
99
−8.773
56.562
48.674
1.00
73.21


ATOM
490
CE1
HIS
A
99
−8.397
57.853
50.407
1.00
72.77


ATOM
491
NE2
HIS
A
99
−8.709
56.621
50.044
1.00
73.04


ATOM
492
N
LEU
A
100
−6.195
55.700
46.424
1.00
69.36


ATOM
493
CA
LEU
A
100
−6.136
54.273
46.269
1.00
69.47


ATOM
494
C
LEU
A
100
−5.759
53.618
47.587
1.00
72.05


ATOM
495
O
LEU
A
100
−4.826
54.047
48.264
1.00
71.58


ATOM
496
CB
LEU
A
100
−5.152
53.899
45.156
1.00
69.88


ATOM
497
CG
LEU
A
100
−5.715
54.059
43.740
1.00
74.87


ATOM.
498
CD1
LEU
A
100
−4.638
53.907
42.702
1.00
75.16


ATOM
499
CD2
LEU
A
100
−6.788
53.017
43.537
1.00
77.41


ATOM
500
N
GLU
A
101
−6.536
52.616
47.975
1.00
67.74


ATOM
501
CA
GLU
A
101
−6.297
51.895
49.212
1.00
66.94


ATOM
502
C
GLU
A
101
−5.574
50.601
48.896
1.00
70.57


ATOM
503
O
GLU
A
101
−6.173
49.641
48.405
1.00
70.21


ATOM
504
CB
GLU
A
101
−7.613
51.607
49.927
1.00
68.11


ATOM
505
CG
GLU
A
101
−8.499
52.823
50.096
1.00
79.60


ATOM
506
CD
GLU
A
101
−8.304
53.508
51.433
1.00
100.23


ATOM
507
OE1
GLU
A
101
−8.902
53.045
52.427
1.00
98.33


ATOM
508
OE2
GLU
A
101
−7.546
54.506
51.492
1.00
90.20


ATOM
509
N
ILE
A
102
−4.267
50.597
49.126
1.00
67.43


ATOM
510
CA
ILE
A
102
−3.457
49.427
48.846
1.00
67.73


ATOM
511
C
ILE
A
102
−2.258
49.297
49.824
1.00
73.57


ATOM
512
O
ILE
A
102
−2.155
50.098
50.751
1.00
73.54


ATOM
513
CB
ILE
A
102
−2.923
49.440
47.407
1.00
70.85


ATOM
514
CG1
ILE
A
102
−3.689
50.462
46.572
1.00
71.05


ATOM
515
CG2
ILE
A
102
−3.045
48.058
46.783
1.00
71.85


ATOM
516
CD1
ILE
A
102
−4.219
49.911
45.264
1.00
77.53


ATOM
517
N
LYS
A
103
−1.486
48.266
49.626
1.00
72.51


ATOM
518
CA
LYS
A
103
−0.361
47.989
50.509
1.00
72.51


ATOM
519
C
LYS
A
103
0.877
48.810
50.159
1.00
76.53


ATOM
520
O
LYS
A
103
1.058
49.227
49.019
1.00
77.01


ATOM
521
CB
LYS
A
103
−0.038
46.499
50.495
1.00
75.85


ATOM
522
CG
LYS
A
103
−1.119
45.642
49.860
1.00
94.42


ATOM
523
CD
LYS
A
103
−0.951
44.177
50.220
1.00
107.25


ATOM
524
CE
LYS
A
103
−2.102
43.681
51.084
1.00
117.44


ATOM
525
NZ
LYS
A
103
−2.032
42.213
51.315
1.00
124.08


ATOM
526
N
PRO
A
104
1.722
49.042
51.159
1.00
73.79


ATOM
527
CA
PRO
A
104
2.949
49.811
50.978
1.00
73.09


ATOM
528
C
PRO
A
104
3.787
49.249
49.841
1.00
77.39


ATOM
529
O
PRO
A
104
4.330
49.996
49.029
1.00
77.24


ATOM
530
CB
PRO
A
104
3.685
49.633
52.324
1.00
74.50


ATOM
531
CG
PRO
A
104
2.870
48.627
53.107
1.00
78.72


ATOM
532
CD
PRO
A
104
1.499
48.688
52.567
1.00
73.39


ATOM
533
N
ALA
A
105
3.898
47.927
49.796
1.00
75.03


ATOM
534
CA
ALA
A
105
4.639
47.265
48.739
1.00
75.11


ATOM
535
C
ALA
A
105
4.032
47.686
47.406
1.00
80.14


ATOM
536
O
ALA
A
105
4.726
48.214
46.536
1.00
80.02


ATOM
537
CB
ALA
A
105
4.557
45.764
48.904
1.00
75.76


ATOM
538
N
ILE
A
106
2.722
47.483
47.268
1.00
76.82


ATOM
539
CA
ILE
A
106
2.010
47.866
46.061
1.00
76.79


ATOM
540
C
ILE
A
106
2.295
49.330
45.713
1.00
78.22


ATOM
541
O
ILE
A
106
2.975
49.633
44.724
1.00
77.84


ATOM
542
CB
ILE
A
106
0.476
47.704
46.224
1.00
80.90


ATOM
543
CG1
ILE
A
106
0.108
46.231
46.387
1.00
81.84


ATOM
544
CG2
ILE
A
106
−0.260
48.317
45.041
1.00
82.10


ATOM
545
CD1
ILE
A
106
−1.243
45.865
45.768
1.00
89.96


ATOM
546
N
ARG
A
107
1.760
50.234
46.533
1.00
72.72


ATOM
547
CA
ARG
A
107
1.911
51.665
46.308
1.00
71.63


ATOM
548
C
ARG
A
107
3.349
52.087
45.979
1.00
74.51


ATOM
549
O
ARG
A
107
3.571
52.964
45.133
1.00
72.76


ATOM
550
CB
ARG
A
107
1.403
52.450
47.521
1.00
71.16


ATOM
551
CG
ARG
A
107
2.479
53.204
48.268
1.00
81.38


ATOM
552
CD
ARG
A
107
2.130
53.365
49.736
1.00
92.32


ATOM
553
NE
ARG
A
107
3.320
53.530
50.573
1.00
101.91


ATOM
554
CZ
ARG
A
107
3.317
53.454
51.902
1.00
116.20


ATOM
555
NH1
ARG
A
107
2.187
53.220
52.556
1.00
102.19


ATOM
556
NH2
ARG
A
107
4.448
53.608
52.577
1.00
104.27


ATOM
557
N
ASN
A
108
4.317
51.483
46.652
1.00
71.33


ATOM
558
CA
ASN
A
108
5.721
51.847
46.442
1.00
70.99


ATOM
559
C
ASN
A
108
6.278
51.467
45.060
1.00
72.52


ATOM
560
O
ASN
A
108
7.380
51.883
44.690
1.00
71.66


ATOM
561
CB
ASN
A
108
6.609
51.318
47.576
1.00
72.72


ATOM
562
CG
ASN
A
108
6.612
52.237
48.795
1.00
96.36


ATOM
563
OD1
ASN
A
108
7.074
53.379
48.728
1.00
93.42


ATOM
564
ND2
ASN
A
108
6.114
51.733
49.916
1.00
87.85


ATOM
565
N
GLN
A
109
5.496
50.712
44.290
1.00
67.26


ATOM
566
CA
GLN
A
109
5.894
50.316
42.942
1.00
66.00


ATOM
567
C
GLN
A
109
5.429
51.359
41.938
1.00
67.49


ATOM
568
O
GLN
A
109
6.130
51.670
40.968
1.00
66.18


ATOM
569
CB
GLN
A
109
5.313
48.945
42.583
1.00
67.37


ATOM
570
CG
GLN
A
109
6.291
48.031
41.849
1.00
85.26


ATOM
571
CD
GLN
A
109
5.603
46.913
41.102
1.00
113.16


ATOM
572
OE1
GLN
A
109
5.712
45.743
41.460
1.00
112.08


ATOM
573
NE2
GLN
A
109
4.894
47.256
40.021
1.00
105.49


ATOM
574
N
ILE
A
110
4.243
51.898
42.180
1.00
61.59


ATOM
575
CA
ILE
A
110
3.692
52.925
41.319
1.00
60.51


ATOM
576
C
ILE
A
110
4.658
54.114
41.295
1.00
61.99


ATOM
577
O
ILE
A
110
5.067
54.572
40.232
1.00
61.45


ATOM
578
CB
ILE
A
110
2.281
53.359
41.789
1.00
63.40


ATOM
579
CG1
ILE
A
110
1.304
52.178
41.667
1.00
63.33


ATOM
580
CG2
ILE
A
110
1.782
54.541
40.972
1.00
63.89


ATOM
581
CD1
ILE
A
110
0.053
52.316
42.486
1.00
68.43


ATOM
582
N
ILE
A
111
5.092
54.547
42.471
1.00
57.23


ATOM
583
CA
ILE
A
111
6.042
55.649
42.565
1.00
56.82


ATOM
584
C
ILE
A
111
7.316
55.353
41.776
1.00
61.58


ATOM
585
O
ILE
A
111
7.917
56.250
41.181
1.00
61.05


ATOM
586
CB
ILE
A
111
6.374
55.988
44.022
1.00
59.36


ATOM
587
CG1
ILE
A
111
5.154
56.602
44.696
1.00
59.69


ATOM
588
CG2
ILE
A
111
7.546
56.940
44.097
1.00
59.55


ATOM
589
CD1
ILE
A
111
4.195
57.264
43.720
1.00
66.02


ATOM
590
N
ARG
A
112
7.697
54.084
41.738
1.00
59.00


ATOM
591
CA
ARG
A
112
8.878
53.661
40.994
1.00
59.12


ATOM
592
C
ARG
A
112
8.645
53.791
39.483
1.00
62.26


ATOM
593
O
ARG
A
112
9.489
54.336
38.758
1.00
61.96


ATOM
594
CB
ARG
A
112
9.228
52.209
41.341
1.00
60.96


ATOM
595
CG
ARG
A
112
10.469
52.052
42.208
1.00
77.00


ATOM
596
CD
ARG
A
112
10.677
50.588
42.608
1.00
93.15


ATOM
597
NE
ARG
A
112
10.595
49.693
41.455
1.00
106.58


ATOM
598
CZ
ARG
A
112
10.691
48.368
41.526
1.00
125.06


ATOM
599
NH1
ARG
A
112
10.867
47.774
42.698
1.00
115.82


ATOM
600
NH2
ARG
A
112
10.606
47.638
40.422
1.00
112.74


ATOM
601
N
GLU
A
113
7.505
53.270
39.017
1.00
57.70


ATOM
602
CA
GLU
A
113
7.151
53.296
37.595
1.00
56.82


ATOM
603
C
GLU
A
113
6.854
54.707
37.059
1.00
59.02


ATOM
604
O
GLU
A
113
6.978
54.959
35.865
1.00
58.49


ATOM
605
CB
GLU
A
113
5.956
52.376
37.309
1.00
58.24


ATOM
606
CG
GLU
A
113
5.844
51.164
38.209
1.00
68.55


ATOM
607
CD
GLU
A
113
4.732
50.211
37.776
1.00
85.71


ATOM
608
OE1
GLU
A
113
3.640
50.692
37.395
1.00
77.08


ATOM
609
OE2
GLU
A
113
4.947
48.982
37.825
1.00
77.74


ATOM
610
N
LEU
A
113
6.431
55.611
37.936
1.00
53.89


ATOM
611
CA
LEU
A
114
6.132
56.977
37.516
1.00
52.90


ATOM
612
C
LEU
A
114
7.407
57.789
37.379
1.00
56.80


ATOM
613
O
LEU
A
114
7.418
58.841
36.729
1.00
56.28


ATOM
614
CB
LEU
A
114
5.186
57.645
38.504
1.00
52.64


ATOM
615
CG
LEU
A
114
3.868
56.907
38.682
1.00
56.55


ATOM
616
CD1
LEU
A
114
3.148
57.377
39.935
1.00
56.39


ATOM
617
CD2
LEU
A
114
3.005
57.086
37.443
1.00
57.76


ATOM
618
N
GLN
A
115
8.486
57.291
37.981
1.00
52.83


ATOM
619
CA
GLN
A
115
9.774
57.967
37.927
1.00
52.37


ATOM
620
C
GLN
A
115
10.269
58.104
36.491
1.00
55.50


ATOM
621
O
GLN
A
115
11.180
58.878
36.217
1.00
55.32


ATOM
622
CB
GLN
A
115
10.810
57.238
38.791
1.00
53.59


ATOM
623
CG
GLN
A
115
10.427
57.132
40.263
1.00
54.80


ATOM
624
CD
GLN
A
115
10.216
58.483
40.902
1.00
61.23


ATOM
625
OE1
GLN
A
115
11.098
59.342
40.869
1.00
59.16


ATOM
626
NE2
GLN
A
115
9.031
58.696
41.455
1.00
41.92


ATOM
627
N
VAL
A
116
9.657
57.355
35.579
1.00
51.56


ATOM
628
CA
VAL
A
116
10.005
57.428
34.158
1.00
51.35


ATOM
629
C
VAL
A
116
9.640
58.794
33.586
1.00
52.54


ATOM
630
O
VAL
A
116
10.222
59.242
32.599
1.00
51.86


ATOM
631
CB
VAL
A
116
9.249
56.367
33.342
1.00
56.11


ATOM
632
CG1
VAL
A
116
9.941
56.138
32.004
1.00
56.23


ATOM
633
CG2
VAL
A
116
9.155
55.080
34.121
1.00
56.24


ATOM
634
N
LEU
A
117
8.672
59.446
34.219
1.00
47.59


ATOM
635
CA
LEU
A
117
8.201
60.754
33.785
1.00
46.57


ATOM
636
C
LEU
A
117
9.276
61.818
33.873
1.00
50.07


ATOM
637
O
LEU
A
117
9.180
62.865
33.231
1.00
49.38


ATOM
638
CB
LEU
A
117
6.977
61.169
34.593
1.00
46.36


ATOM
639
CG
LEU
A
117
5.731
60.324
34.364
1.00
50.06


ATOM
640
CD1
LEU
A
117
4.693
60.614
35.432
1.00
50.24


ATOM
641
CD2
LEU
A
117
5.177
60.583
32.984
1.00
51.33


ATOM
642
N
HIS
A
118
10.301
61.561
34.670
1.00
47.18


ATOM
643
CA
HIS
A
118
11.396
62.515
34.811
1.00
47.41


ATOM
644
C
HIS
A
118
12.232
62.566
33.533
1.00
52.13


ATOM
645
O
HIS
A
118
12.989
63.511
33.314
1.00
51.97


ATOM
646
CB
HIS
A
118
12.289
62.147
36.008
1.00
48.10


ATOM
647
CO
HIS
A
118
11.707
62.526
37.334
1.00
51.12


ATOM
648
ND1
HIS
A
118
11.296
61.590
38.261
1.00
52.58


ATOM
649
CD2
HIS
A
118
11.483
63.737
37.896
1.00
52.57


ATOM
650
CE1
HIS
A
118
10.836
62.211
39.332
1.00
51.91


ATOM
651
NE2
HIS
A
118
10.944
63.514
39.138
1.00
52.19


ATOM
652
N
GLU
A
119
12.067
61.552
32.685
1.00
48.86


ATOM
653
CA
GLU
A
119
12.813
61.457
31.435
1.00
48.84


ATOM
654
C
GLU
A
119
12.085
62.056
30.229
1.00
53.33


ATOM
655
O
GLU
A
119
12.709
62.362
29.212
1.00
52.81


ATOM
656
CB
GLU
A
119
13.161
59.998
31.141
1.00
50.25


ATOM
657
CG
GLU
A
119
14.024
59.327
32.205
1.00
62.42


ATOM
658
CD
GLU
A
119
13.956
57.806
32.131
1.00
86.20


ATOM
659
OE1
GLU
A
119
14.395
57.236
31.106
1.00
73.89


ATOM
660
OE2
GLU
A
119
13.446
57.183
33.090
1.00
84.10


ATOM
661
N
CYS
A
120
10.764
62.178
30.325
1.00
50.32


ATOM
662
CA
CYS
A
120
9.962
62.704
29.210
1.00
50.21


ATOM
663
C
CYS
A
120
10.052
64.211
29.105
1.00
52.71


ATOM
664
O
CYS
A
120
9.202
64.926
29.630
1.00
52.94


ATOM
665
CB
CYS
A
120
8.502
62.277
29.347
1.00
50.58


ATOM
666
SG
CYS
A
120
8.292
60.491
29.563
1.00
54.74


ATOM
667
N
ASN
A
121
11.064
64.689
28.397
1.00
47.69


ATOM
668
CA
ASN
A
121
11.270
66.124
28.230
1.00
47.26


ATOM
669
C
ASN
A
121
11.030
66.579
26.794
1.00
48.76


ATOM
670
O
ASN
A
121
11.838
66.317
25.901
1.00
48.20


ATOM
671
CB
ASN
A
121
12.675
66.512
28.696
1.00
50.37


ATOM
672
CG
ASN
A
121
12.992
65.972
30.089
1.00
75.62


ATOM
673
OD1
ASN
A
121
12.250
66.219
31.044
1.00
64.39


ATOM
674
ND2
ASN
A
121
14.059
65.176
30.191
1.00
68.30


ATOM
675
N
SER
A
122
9.907
67.256
26.577
1.00
43.39


ATOM
676
CA
SER
A
122
9.541
67.724
25.246
1.00
41.91


ATOM
677
C
SER
A
122
8.528
68.877
25.323
1.00
44.18


ATOM
678
O
SER
A
122
7.746
68.964
26.264
1.00
43.27


ATOM
679
CB
SER
A
122
8.995
66.551
24.409
1.00
43.95


ATOM
680
OG
SER
A
122
7.961
66.953
23.538
1.00
49.97


ATOM
681
N
PRO
A
123
8.580
69.778
24.345
1.00
40.17


ATOM
682
CA
PRO
A
123
7.669
70.919
24.300
1.00
39.21


ATOM
683
C
PRO
A
123
6.224
70.465
24.103
1.00
41.77


ATOM
684
O
PRO
A
123
5.293
71.268
24.206
1.00
41.64


ATOM
685
CB
PRO
A
123
8.137
71.694
23.053
1.00
41.09


ATOM
686
CO
PRO
A
123
9.503
71.158
22.737
1.00
45.37


ATOM
687
CD
PRO
A
123
9.492
69.747
23.189
1.00
40.61


ATOM
688
N
TYR
A
124
6.040
69.179
23.816
1.00
37.24


ATOM
689
CA
TYR
A
124
4.702
68.628
23.569
1.00
36.67


ATOM
690
C
TYR
A
124
4.249
67.687
24.659
1.00
41.42


ATOM
691
O
TYR
A
124
3.237
66.987
24.514
1.00
41.30


ATOM
692
CB
TYR
A
124
4.657
67.946
22.204
1.00
37.42


ATOM
693
CG
TYR
A
124
5.231
68.824
21.124
1.00
37.87


ATOM
694
CD1
TYR
A
124
4.567
69.977
20.723
1.00
39.17


ATOM
695
CD2
TYR
A
124
6.507
68.594
20.619
1.00
37.95


ATOM
696
CE1
TYR
A
124
5.103
70.810
19.766
1.00
39.06


ATOM
697
CE2
TYR
A
124
7.057
69.435
19.677
1.00
38.38


ATOM
698
CZ
TYR
A
124
6.355
70.553
19.265
1.00
45.52


ATOM
699
OH
TYR
A
124
6.903
71.411
18.337
1.00
47.09


ATOM
700
N
ILE
A
125
4.989
67.690
25.769
1.00
37.81


ATOM
701
CA
ILE
A
125
4.670
66.845
26.913
1.00
37.65


ATOM
702
C
ILE
A
125
4.612
67.719
28.158
1.00
43.81


ATOM
703
O
ILE
A
125
5.520
68.512
28.402
1.00
43.56


ATOM
704
CB
ILE
A
125
5.744
65.753
27.121
1.00
40.25


ATOM
705
CG1
ILE
A
125
5.834
64.833
25.890
1.00
40.12


ATOM
706
CG2
ILE
A
125
5.458
64.951
28.385
1.00
41.01


ATOM
707
CD1
ILE
A
125
4.514
64.263
25.453
1.00
40.73


ATOM
708
N
VAL
A
126
3.530
67.611
28.928
1.00
41.82


ATOM
709
CA
VAL
A
126
3.408
68.423
30.133
1.00
42.51


ATOM
710
C
VAL
A
126
4.595
68.140
31.063
1.00
46.54


ATOM
711
O
VAL
A
126
5.025
66.996
31.200
1.00
45.10


ATOM
712
CB
VAL
A
126
2.077
68.163
30.890
1.00
46.85


ATOM
713
CG1
VAL
A
126
1.799
69.287
31.871
1.00
46.53


ATOM
714
CG2
VAL
A
126
0.925
68.018
29.909
1.00
46.80


ATOM
715
N
GLY
A
127
5.135
69.196
31.671
1.00
44.10


ATOM
716
CA
GLY
A
127
6.263
69.066
32.589
1.00
43.71


ATOM
717
C
GLY
A
127
5.878
68.229
33.804
1.00
47.33


ATOM
718
O
GLY
A
127
4.779
68.365
34.346
1.00
46.64


ATOM
719
N
PHE
A
128
6.784
67.351
34.218
1.00
43.59


ATOM
720
CA
PHE
A
128
6.558
66.490
35.380
1.00
42.86


ATOM
721
C
PHE
A
128
7.515
66.884
36.495
1.00
47.07


ATOM
722
O
PHE
A
128
8.725
66.967
36.281
1.00
46.77


ATOM
723
CB
PHE
A
128
6.779
65.025
34.996
1.00
44.16


ATOM
724
CG
PHE
A
128
6.739
64.072
36.158
1.00
45.61


ATOM
725
CD1
PHE
A
128
5.537
63.762
36.782
1.00
49.00


ATOM
726
CD2
PHE
A
128
7.894
63.431
36.589
1.00
47.42


ATOM
727
CE1
PHE
A
128
5.498
62.848
37.836
1.00
49.74


ATOM
728
CE2
PHE
A
128
7.857
62.529
37.640
1.00
50.12


ATOM
729
CZ
PHE
A
128
6.660
62.239
38.263
1.00
48.38


ATOM
730
N
TYR
A
129
6.972
67.117
37.686
1.00
44.43


ATOM
731
CA
TYR
A
129
7.787
67.486
38.851
1.00
43.79


ATOM
732
C
TYR
A
129
8.154
66.286
39.709
1.00
49.78


ATOM
733
O
TYR
A
129
9.276
66.180
40.196
1.00
50.15


ATOM
734
CB
TYR
A
129
7.081
68.541
39.689
1.00
43.79


ATOM
735
CG
TYR
A
129
7.211
69.905
39.099
1.00
44.23


ATOM
736
CD1
TYR
A
129
8.460
70.460
38.877
1.00
46.30


ATOM
737
CD2
TYR
A
129
6.095
70.605
38.664
1.00
44.27


ATOM
738
CE1
TYR
A
129
8.593
71.695
38.291
1.00
46.93


ATOM
739
CE2
TYR
A
129
6.219
71.841
38.078
1.00
44.72


ATOM
740
CZ
TYR
A
129
7.473
72.377
37.884
1.00
50.88


ATOM
741
OH
TYR
A
129
7.611
73.610
37.297
1.00
51.44


ATOM
742
N
GLY
A
130
7.202
65.384
39.895
1.00
47.06


ATOM
743
CA
GLY
A
130
7.446
64.195
40.692
1.00
47.15


ATOM
744
C
GLY
A
130
6.140
63.591
41.166
1.00
51.79


ATOM
745
O
GLY
A
130
5.058
64.097
40.848
1.00
50.86


ATOM
746
N
ALA
A
131
6.248
62.506
41.929
1.00
49.48


ATOM
747
CA
ALA
A
131
5.082
61.809
42.455
1.00
49.81


ATOM
748
C
ALA
A
131
5.401
61.157
43.794
1.00
53.55


ATOM
749
O
ALA
A
131
6.511
60.668
44.016
1.00
53.41


ATOM
750
CB
ALA
A
131
4.592
60.760
41.455
1.00
50.77


ATOM
751
N
PHE
A
132
4.409
61.124
44.674
1.00
49.57


ATOM
752
CA
PHE
A
132
4.587
60.551
45.997
1.00
49.08


ATOM
753
C
PHE
A
132
3.258
60.050
46.544
1.00
54.20


ATOM
754
O
PHE
A
132
2.194
60.357
46.001
1.00
53.07


ATOM
755
CB
PHE
A
132
5.173
61.607
46.944
1.00
50.30


ATOM
756
CG
PHE
A
132
4.330
62.850
47.065
1.00
51.35


ATOM
757
CD1
PHE
A
132
4.439
63.878
46.132
1.00
54.16


ATOM
758
CD2
PHE
A
132
3.415
62.987
48.098
1.00
53.08


ATOM
759
CE1
PHE
A
132
3.671
65.020
46.245
1.00
54.79


ATOM
760
CE2
PHE
A
132
2.643
64.134
48.216
1.00
55.52


ATOM
761
CZ
PHE
A
132
2.770
65.148
47.292
1.00
53.59


ATOM
762
N
TYR
A
133
3.325
59.276
47.623
1.00
52.56


ATOM
763
CA
TYR
A
133
2.127
58.753
48.266
1.00
53.32


ATOM
764
C
TYR
A
133
1.929
59.416
49.621
1.00
58.10


ATOM
765
O
TYR
A
133
2.897
59.819
50.270
1.00
57.69


ATOM
766
CB
TYR
A
133
2.214
57.236
48.445
1.00
55.00


ATOM
767
CG
TYR
A
133
1.042
56.663
49.205
1.00
57.28


ATOM
768
CD1
TYR
A
133
1.075
56.521
50.583
1.00
59.29


ATOM
769
CD2
TYR
A
133
−0.153
56.352
48.542
1.00
58.33


ATOM
770
CE1
TYR
A
133
−0.039
56.076
51.285
1.00
60.44


ATOM
771
CE2
TYR
A
133
−1.230
55.829
49.230
1.00
59.52


ATOM
772
CZ
TYR
A
133
−1.186
55.719
50.600
1.00
69.38


ATOM
773
OH
TYR
A
133
−2.250
55.192
51.273
1.00
73.84


ATOM
774
N
SER
A
134
0.682
59.532
50.055
1.00
55.13


ATOM
775
CA
SER
A
134
0.412
60.145
51.334
1.00
55.40


ATOM
776
C
SER
A
134
−1.021
59.993
51.785
1.00
60.42


ATOM
777
O
SER
A
134
−1.954
60.432
51.110
1.00
59.61


ATOM
778
CB
SER
A
134
0.821
61.622
51.326
1.00
59.40


ATOM
779
OG
SER
A
134
0.468
62.256
52.551
1.00
69.83


ATOM
780
N
ASP
A
135
−1.183
59.382
52.948
1.00
58.60


ATOM
781
CA
ASP
A
135
−2.480
59.192
53.571
1.00
59.21


ATOM
782
C
ASP
A
135
−3.616
58.772
52.629
1.00
64.13


ATOM
783
O
ASP
A
135
−4.631
59.464
52.500
1.00
63.53


ATOM
784
CB
ASP
A
135
−2.853
60.403
54.427
1.00
61.52


ATOM
785
CG
ASP
A
135
−2.071
60.450
55.755
1.00
74.92


ATOM
786
OD1
ASP
A
135
−2.093
61.506
56.423
1.00
76.12


ATOM
787
OD2
ASP
A
135
−1.401
59.440
56.096
1.00
80.38


ATOM
788
N
GLY
A
136
−3.445
57.603
52.009
1.00
61.13


ATOM
789
CA
GLY
A
136
−4.468
57.005
51.162
1.00
60.95


ATOM
790
C
GLY
A
136
−4.607
57.575
49.759
1.00
64.42


ATOM
791
O
GLY
A
136
−5.601
57.316
49.082
1.00
64.83


ATOM
792
N
GLU
A
137
−3.622
58.330
49.299
1.00
59.33


ATOM
793
CA
GLU
A
137
−3.712
58.881
47.955
1.00
58.24


ATOM
794
C
GLU
A
137
−2.383
59.097
47.274
1.00
58.50


ATOM
795
O
GLU
A
137
−1.388
59.442
47.913
1.00
57.81


ATOM
796
CB
GLU
A
137
−4.534
60.167
47.938
1.00
59.80


ATOM
797
CG
GLU
A
137
−4.123
61.171
48.986
1.00
72.29


ATOM
798
CD
GLU
A
137
−5.137
62.270
49.153
1.00
92.13


ATOM
799
OE1
GLU
A
137
−6.194
62.208
48.489
1.00
84.42


ATOM
800
OE2
GLU
A
137
−4.877
63.201
49.941
1.00
87.23


ATOM
801
N
ILE
A
138
−2.376
58.905
45.958
1.00
52.47


ATOM
802
CA
ILE
A
138
−1.178
59.116
45.166
1.00
50.72


ATOM
803
C
ILE
A
138
−1.193
60.507
44.575
1.00
51.38


ATOM
804
O
ILE
A
138
−2.237
60.997
44.138
1.00
50.50


ATOM
805
CB
ILE
A
138
−1.068
58.112
44.027
1.00
53.50


ATOM
806
CG1
ILE
A
138
−0.862
56.706
44.583
1.00
53.99


ATOM
807
CG2
ILE
A
138
0.086
58.484
43.122
1.00
53.75


ATOM
808
CD1
ILE
A
138
0.582
56.276
44.598
1.00
61.13


ATOM
809
N
SER
A
139
−0.030
61.138
44.539
1.00
46.19


ATOM
810
CA
SER
A
139
0.074
62.478
44.010
1.00
44.93


ATOM
811
C
SER
A
139
1.003
62.542
42.818
1.00
47.92


ATOM
812
O
SER
A
139
2.130
62.031
42.858
1.00
47.10


ATOM
813
CB
SER
A
139
0.550
63.454
45.098
1.00
47.17


ATOM
814
OG
SER
A
139
−0.547
63.997
45.807
1.00
53.47


ATOM
815
N
ILE
A
140
0.533
63.192
41.759
1.00
43.79


ATOM
816
CA
ILE
A
140
1.338
63.406
40.568
1.00
43.06


ATOM
817
C
ILE
A
140
1.356
64.899
40.318
1.00
45.06


ATOM
818
O
ILE
A
140
0.322
65.513
40.066
1.00
43.65


ATOM
819
CB
ILE
A
140
0.780
62.650
39.336
1.00
46.38


ATOM
820
CG1
ILE
A
140
1.122
61.161
39.430
1.00
47.27


ATOM
821
CG2
ILE
A
140
1.361
63.222
38.049
1.00
46.44


ATOM
822
CD1
ILE
A
140
−0.048
60.237
39.114
1.00
54.07


ATOM
823
N
CYS
A
141
2.523
65.494
40.491
1.00
41.92


ATOM
824
CA
CYS
A
141
2.673
66.931
40.350
1.00
41.37


ATOM
825
C
CYS
A
141
3.306
67.246
39.037
1.00
44.11


ATOM
826
O
CYS
A
141
4.328
66.673
38.673
1.00
43.30


ATOM
827
CB
CYS
A
141
3.514
67.503
41.491
1.00
41.47


ATOM
828
SG
CYS
A
141
2.917
67.011
43.134
1.00
45.33


ATOM
829
N
MET
A
142
2.693
68.157
38.317
1.00
41.01


ATOM
830
CA
MET
A
142
3.184
68.509
37.025
1.00
40.77


ATOM
831
C
MET
A
142
3.114
69.995
36.811
1.00
44.64


ATOM
832
O
MET
A
142
2.656
70.741
37.672
1.00
44.26


ATOM
833
CB
MET
A
142
2.369
67.779
35.954
1.00
42.80


ATOM
834
CG
MET
A
142
0.877
67.976
36.092
1.00
46.11


ATOM
835
SD
MET
A
142
−0.130
66.649
35.338
1.00
49.61


ATOM
836
CE
MET
A
142
−1.417
66.463
36.638
1.00
46.04


ATOM
837
N
GLU
A
143
3.591
70.419
35.656
1.00
41.37


ATOM
838
CA
GLU
A
143
3.551
71.805
35.280
1.00
40.86


ATOM
839
C
GLU
A
143
2.076
72.195
35.161
1.00
43.89


ATOM
840
O
GLU
A
143
1.234
71.375
34.782
1.00
43.80


ATOM
841
CB
GLU
A
143
4.279
71.992
33.945
1.00
42.11


ATOM
842
CG
GLU
A
143
3.706
73.050
33.054
1.00
49.11


ATOM
843
CD
GLU
A
143
4.311
73.016
31.667
1.00
59.88


ATOM
844
OE1
GLU
A
143
4.679
71.916
31.201
1.00
43.12


ATOM
845
OE2
GLU
A
143
4.432
74.086
31.048
1.00
54.40


ATOM
846
N
HIS
A
144
1.757
73.416
35.562
1.00
39.12


ATOM
847
CA
HIS
A
144
0.388
73.888
35.508
1.00
38.36


ATOM
848
C
HIS
A
144
0.113
74.585
34.166
1.00
41.61


ATOM
849
O
HIS
A
144
0.808
75.529
33.796
1.00
41.90


ATOM
850
CB
HIS
A
144
0.098
74.826
36.681
1.00
38.74


ATOM
851
CG
HIS
A
144
−1.086
75.715
36.465
1.00
42.25


ATOM
852
ND1
HIS
A
144
−2.385
75.276
36.618
1.00
44.04


ATOM
853
CD2
HIS
A
144
−1.169
77.020
36.116
1.00
43.89


ATOM
854
CE1
HIS
A
144
−3.216
76.273
36.377
1.00
43.31


ATOM
855
NE2
HIS
A
144
−2.504
77.339
36.059
1.00
43.63


ATOM
856
N
MET
A
145
−0.883
74.080
33.433
1.00
36.14


ATOM
857
CA
MET
A
145
−1.266
74.637
32.144
1.00
34.97


ATOM
858
C
MET
A
145
−2.480
75.551
32.333
1.00
40.53


ATOM
859
O
MET
A
145
−3.611
75.092
32.509
1.00
39.97


ATOM
860
CB
MET
A
145
−1.560
73.514
31.141
1.00
36.54


ATOM
861
CG
MET
A
145
−0.373
72.580
30.868
1.00
38.92


ATOM
862
SD
MET
A
145
1.040
73.396
30.042
1.00
42.32


ATOM
863
CE
MET
A
145
0.443
73.464
28.312
1.00
38.55


ATOM
864
N
ASP
A
146
−2.217
76.851
32.351
1.00
37.99


ATOM
865
CA
ASP
A
146
−3.246
77.860
32.640
1.00
37.56


ATOM
866
C
ASP
A
146
−4.436
77.871
31.680
1.00
40.10


ATOM
867
O
ASP
A
146
−5.485
78.440
31.985
1.00
39.53


ATOM
868
CB
ASP
A
146
−2.605
79.250
32.700
1.00
38.84


ATOM
869
CG
ASP
A
146
−1.977
79.646
31.394
1.00
46.28


ATOM
870
OD1
ASP
A
146
−1.945
78.804
30.459
1.00
45.95


ATOM
871
OD2
ASP
A
146
−1.546
80.806
31.278
1.00
51.89


ATOM
872
N
GLY
A
147
−4.272
77.259
30.515
1.00
35.63


ATOM
873
CA
GLY
A
147
−5.339
77.249
29.516
1.00
34.67


ATOM
874
C
GLY
A
147
−6.289
76.084
29.732
1.00
37.16


ATOM
875
O
GLY
A
147
−7.334
76.002
29.088
1.00
36.07


ATOM
876
N
GLY
A
148
−5.918
75.187
30.652
1.00
33.70


ATOM
877
CA
GLY
A
148
−6.728
74.015
30.978
1.00
32.98


ATOM
878
C
GLY
A
148
−6.627
72.966
29.868
1.00
36.75


ATOM
879
O
GLY
A
148
−5.662
72.956
29.094
1.00
36.57


ATOM
880
N
SER
A
149
−7.642
72.110
29.782
1.00
32.82


ATOM
881
CA
SER
A
149
−7.708
71.057
28.763
1.00
32.05


ATOM
882
C
SER
A
149
−8.647
71.454
27.588
1.00
36.07


ATOM
883
O
SER
A
149
−9.516
72.322
27.733
1.00
35.33


ATOM
884
CB
SER
A
149
−8.174
69.751
29.396
1.00
33.58


ATOM
885
OG
SER
A
149
−9.369
69.949
30.136
1.00
38.62


ATOM
886
N
LEU
A
150
−8.467
70.810
26.437
1.00
32.55


ATOM
887
CA
LEU
A
150
−9.244
71.137
25.239
1.00
32.31


ATOM
888
C
LEU
A
150
−10.750
70.888
25.339
1.00
36.42


ATOM
889
O
LEU
A
150
−11.534
71.520
24.634
1.00
35.66


ATOM
890
CB
LEU
A
150
−8.634
70.506
23.984
1.00
32.30


ATOM
891
CG
LEU
A
150
−7.369
71.198
23.442
1.00
36.21


ATOM
892
CD1
LEU
A
150
−7.008
70.655
22.075
1.00
35.91


ATOM
893
CD2
LEU
A
150
−7.556
72.714
23.382
1.00
37.50


ATOM
894
N
ASP
A
151
−11.160
69.992
26.233
1.00
33.52


ATOM
895
CA
ASP
A
151
−12.577
69.768
26.441
1.00
33.51


ATOM
896
C
ASP
A
151
−13.161
71.014
27.074
1.00
36.74


ATOM
897
O
ASP
A
151
−14.232
71.470
26.696
1.00
36.96


ATOM
898
CB
ASP
A
151
−12.821
68.547
27.333
1.00
35.90


ATOM
899
CG
ASP
A
151
−12.209
68.694
28.704
1.00
45.47


ATOM
900
OD1
ASP
A
151
−12.968
68.645
29.704
1.00
46.19


ATOM
901
OD2
ASP
A
151
−10.969
68.815
28.786
1.00
50.32


ATOM
902
N
GLN
A
152
−12.409
71.613
27.987
1.00
33.29


ATOM
903
CA
GLN
A
152
−12.843
72.844
28.646
1.00
32.60


ATOM
904
C
GLN
A
152
−12.861
73.995
27.664
1.00
37.66


ATOM
905
O
GLN
A
152
−13.781
74.817
27.664
1.00
38.61


ATOM
906
CB
GLN
A
152
−11.928
73.178
29.825
1.00
33.34


ATOM
907
CG
GLN
A
152
−11.983
72.156
30.963
1.00
33.39


ATOM
908
CD
GLN
A
152
−10.850
72.350
31.994
1.00
50.32


ATOM
909
OE1
GLN
A
152
−9.703
72.686
31.643
1.00
43.09


ATOM
910
NE2
GLN
A
152
−11.159
72.089
33.249
1.00
40.91


ATOM
911
N
VAL
A
153
−11.831
74.063
26.827
1.00
33.31


ATOM
912
CA
VAL
A
153
−11.729
75.116
25.841
1.00
32.56


ATOM
913
C
VAL
A
153
−12.864
74.997
24.837
1.00
37.28


ATOM
914
O
VAL
A
153
−13.499
75.995
24.476
1.00
36.74


ATOM
915
CB
VAL
A
153
−10.394
75.038
25.085
1.00
35.93


ATOM
916
CG1
VAL
A
153
−10.335
76.113
23.991
1.00
35.68


ATOM
917
CG2
VAL
A
153
−9.232
75.163
26.051
1.00
35.37


ATOM
918
N
LEU
A
154
−13.086
73.779
24.350
1.00
34.14


ATOM
919
CA
LEU
A
154
−14.161
73.526
23.386
1.00
34.15


ATOM
920
C
LEU
A
154
−15.517
73.952
23.991
1.00
39.48


ATOM
921
O
LEU
A
154
−16.288
74.669
23.368
1.00
38.45


ATOM
922
CB
LEU
A
154
−14.184
72.042
22.993
1.00
33.79


ATOM
923
CG
LEU
A
154
−15.326
71.621
22.070
1.00
37.51


ATOM
924
CD1
LEU
A
154
−15.278
72.417
20.792
1.00
37.43


ATOM
925
CD2
LEU
A
154
−15.312
70.121
21.800
1.00
37.47


ATOM
926
N
LYS
A
155
−15.761
73.539
25.231
1.00
38.36


ATOM
927
CA
LYS
A
155
−16.987
73.900
25.944
1.00
39.40


ATOM
928
C
LYS
A
155
−17.203
75.411
25.925
1.00
44.71


ATOM
929
O
LYS
A
155
−18.323
75.892
25.740
1.00
44.66


ATOM
930
CB
LYS
A
155
−16.906
73.420
27.390
1.00
42.30


ATOM
931
CG
LYS
A
155
−18.211
72.938
27.959
1.00
57.15


ATOM
932
CD
LYS
A
155
−17.974
71.979
29.113
1.00
66.94


ATOM
933
CE
LYS
A
155
−17.010
72.567
30.126
1.00
79.89


ATOM
934
NZ
LYS
A
155
−16.227
71.509
30.834
1.00
90.98


ATOM
935
N
LYS
A
156
−16.120
76.150
26.126
1.00
41.23


ATOM
936
CA
LYS
A
156
−16.166
77.608
26.137
1.00
40.63


ATOM
937
C
LYS
A
156
−16.353
78.189
24.729
1.00
44.10


ATOM
938
O
LYS
A
156
−17.240
78.998
24.501
1.00
43.96


ATOM
939
CB
LYS
A
156
−14.886
78.163
26.772
1.00
42.89


ATOM
940
CG
LYS
A
156
−14.905
79.650
27.021
1.00
59.89


ATOM
941
CD
LYS
A
156
−14.719
79.961
28.498
1.00
68.94


ATOM
942
CE
LYS
A
156
−14.835
81.454
28.760
1.00
81.00


ATOM
943
NZ
LYS
A
156
−14.067
81.870
29.968
1.00
92.98


ATOM
944
N
ALA
A
157
−15.515
77.753
23.790
1.00
39.74


ATOM
945
CA
ALA
A
157
−15.548
78.256
22.416
1.00
38.49


ATOM
946
C
ALA
A
157
−16.761
77.818
21.580
1.00
41.26


ATOM
947
O
ALA
A
157
−17.137
78.501
20.620
1.00
40.70


ATOM
948
CB
ALA
A
157
−14.247
77.899
21.687
1.00
38.84


ATOM
949
N
GLY
A
158
−17.345
76.673
21.909
1.00
37.14


ATOM
950
CA
GLY
A
158
−18.469
76.139
21.129
1.00
36.96


ATOM
951
C
GLY
A
158
−17.865
75.204
20.081
1.00
41.38


ATOM
952
O
GLY
A
158
−18.104
74.007
20.083
1.00
42.77


ATOM
953
N
ARG
A
159
−17.023
75.753
19.235
1.00
36.92


ATOM
954
CA
ARG
A
159
−16.288
74.961
18.277
1.00
36.65


ATOM
955
C
ARG
A
159
−14.970
75.655
17.943
1.00
39.24


ATOM
956
O
ARG
A
159
−14.872
76.874
18.013
1.00
39.10


ATOM
957
CB
ARG
A
159
−17.124
74.621
17.031
1.00
37.51


ATOM
958
CG
ARG
A
159
−17.322
75.742
16.048
1.00
46.30


ATOM
959
CD
ARG
A
159
−18.203
75.265
14.884
1.00
51.91


ATOM
960
NE
ARG
A
159
−18.501
76.341
13.941
1.00
53.90


ATOM
961
CZ
ARG
A
159
−19.721
76.819
13.723
1.00
62.87


ATOM
962
NH1
ARG
A
159
−20.756
76.313
14.372
1.00
47.24


ATOM
963
NH2
ARG
A
159
−19.906
77.800
12.860
1.00
53.08


ATOM
964
N
ILE
A
160
−13.946
74.859
17.668
1.00
34.28


ATOM
965
CA
ILE
A
160
−12.609
75.359
17.403
1.00
33.32


ATOM
966
C
ILE
A
160
−12.289
75.443
15.907
1.00
37.28


ATOM
967
O
ILE
A
160
−12.519
74.484
15.151
1.00
36.77


ATOM
968
CB
ILE
A
160
−11.573
74.493
18.138
1.00
36.08


ATOM
969
CG1
ILE
A
160
−11.992
74.346
19.628
1.00
36.19


ATOM
970
CG2
ILE
A
160
−10.174
75.065
17.975
1.00
35.96


ATOM
971
CD1
ILE
A
160
−10.896
73.862
20.556
1.00
38.32


ATOM
972
N
PRO
A
161
−11.774
76.602
15.478
1.00
32.44


ATOM
973
CA
PRO
A
161
−11.473
76.840
14.058
1.00
31.20


ATOM
974
C
PRO
A
161
−10.402
75.910
13.494
1.00
34.35


ATOM
975
O
PRO
A
161
−9.486
75.486
14.200
1.00
33.66


ATOM
976
CB
PRO
A
161
−11.002
78.306
14.028
1.00
32.50


ATOM
977
CG
PRO
A
161
−11.229
78.838
15.454
1.00
36.42


ATOM
978
CD
PRO
A
161
−11.215
77.657
16.338
1.00
31.84


ATOM
979
N
GLU
A
162
−10.539
75.599
12.215
1.00
31.29


ATOM
980
CA
GLU
A
162
−9.625
74.700
11.520
1.00
31.45


ATOM
981
C
GLU
A
162
−8.145
75.060
11.700
1.00
36.11


ATOM
982
O
GLU
A
162
−7.316
74.186
11.947
1.00
36.02


ATOM
983
CB
GLU
A
162
−9.973
74.650
10.035
1.00
32.70


ATOM
984
CG
GLU
A
162
−9.174
73.641
9.248
1.00
42.08


ATOM
985
CD
GLU
A
162
−9.584
73.590
7.789
1.00
51.46


ATOM
986
OE1
GLU
A
162
−10.786
73.796
7.495
1.00
41.25


ATOM
987
OE2
GLU
A
162
−8.703
73.381
6.937
1.00
39.17


ATOM
988
N
GLN
A
163
−7.818
76.340
11.566
1.00
32.68


ATOM
989
CA
GLN
A
163
−6.433
76.777
11.690
1.00
32.71


ATOM
990
C
GLN
A
163
−5.869
76.489
13.060
1.00
36.07


ATOM
991
O
GLN
A
163
−4.674
76.226
13.206
1.00
35.09


ATOM
992
CB
GLN
A
163
−6.293
78.258
11.352
1.00
34.44


ATOM
993
CG
GLN
A
163
−6.476
78.562
9.867
1.00
44.48


ATOM
994
CD
GLN
A
163
−5.848
79.880
9.455
1.00
55.38


ATOM
995
OE1
GLN
A
163
−5.742
80.808
10.248
1.00
50.52


ATOM
996
NE2
GLN
A
163
−5.440
79.966
8.202
1.00
45.77


ATOM
997
N
ILE
A
164
−6.731
76.550
14.069
1.00
32.65


ATOM
998
CA
ILE
A
164
−6.323
76.259
15.444
1.00
31.80


ATOM
999
C
ILE
A
164
−6.136
74.745
15.562
1.00
34.80


ATOM
1000
O
ILE
A
164
−5.159
74.263
16.150
1.00
34.08


ATOM
1001
CB
ILE
A
164
−7.410
76.730
16.469
1.00
34.51


ATOM
1002
CG1
ILE
A
164
−7.588
78.259
16.411
1.00
34.40


ATOM
1003
CG2
ILE
A
164
−7.056
76.287
17.877
1.00
34.35


ATOM
1004
CD1
ILE
A
164
−6.316
79.053
16.754
1.00
31.27


ATOM
1005
N
LEU
A
165
−7.056
74.004
14.955
1.00
31.21


ATOM
1006
CA
LEU
A
165
−6.993
72.537
14.959
1.00
30.87


ATOM
1007
C
LEU
A
165
−5.770
72.039
14.193
1.00
34.16


ATOM
1008
O
LEU
A
165
−5.235
70.986
14.496
1.00
32.53


ATOM
1009
CB
LEU
A
165
−8.287
71.936
14.408
1.00
30.36


ATOM
1010
CG
LEU
A
165
−9.476
72.143
15.352
1.00
33.55


ATOM
1011
CD1
LEU
A
165
−10.731
71.448
14.833
1.00
33.47


ATOM
1012
CD2
LEU
A
165
−9.119
71.650
16.743
1.00
33.52


ATOM
1013
N
GLY
A
166
−5.295
72.850
13.249
1.00
31.50


ATOM
1014
CA
GLY
A
166
−4.093
72.524
12.496
1.00
31.58


ATOM
1015
C
GLY
A
166
−2.913
72.536
13.458
1.00
36.58


ATOM
1016
O
GLY
A
166
−2.056
71.640
13.430
1.00
37.09


ATOM
1017
N
LYS
A
167
−2.886
73.544
14.325
1.00
32.52


ATOM
1018
CA
LYS
A
167
−1.825
73.680
15.328
1.00
32.54


ATOM
1019
C
LYS
A
167
−1.910
72.549
16.339
1.00
35.59


ATOM
1020
O
LYS
A
167
−0.897
71.973
16.736
1.00
36.00


ATOM
1021
CB
LYS
A
167
−1.943
75.028
16.057
1.00
34.98


ATOM
1022
CG
LYS
A
167
−1.393
76.211
15.279
1.00
42.93


ATOM
1023
CD
LYS
A
167
−0.044
75.904
14.643
1.00
45.73


ATOM
1024
CE
LYS
A
167
0.209
76.830
13.444
1.00
54.67


ATOM
1025
NZ
LYS
A
167
1.593
76.717
12.903
1.00
61.73


ATOM
1026
N
VAL
A
168
−3.122
72.251
16.772
1.00
30.43


ATOM
1027
CA
VAL
A
168
−3.340
71.162
17.697
1.00
29.67


ATOM
1028
C
VAL
A
168
−2.847
69.849
17.089
1.00
33.60


ATOM
1029
O
VAL
A
168
−2.206
69.053
17.758
1.00
34.64


ATOM
1030
CB
VAL
A
168
−4.842
71.007
18.039
1.00
32.67


ATOM
1031
CG1
VAL
A
168
−5.067
69.775
18.875
1.00
31.91


ATOM
1032
CG2
VAL
A
168
−5.363
72.262
18.754
1.00
32.46


ATOM
1033
N
SER
A
169
−3.155
69.626
15.821
1.00
29.10


ATOM
1034
CA
SER
A
169
−2.775
68.386
15.157
1.00
28.48


ATOM
1035
C
SER
A
169
−1.260
68.193
15.198
1.00
33.07


ATOM
1036
O
SER
A
169
−0.761
67.113
15.538
1.00
31.95


ATOM
1037
CB
SER
A
169
−3.280
68.381
13.707
1.00
30.26


ATOM
1038
OG
SER
A
169
−4.690
68.486
13.649
1.00
34.82


ATOM
1039
N
ILE
A
170
−0.535
69.241
14.842
1.00
30.41


ATOM
1040
CA
ILE
A
170
0.907
69.201
14.832
1.00
30.84


ATOM
1041
C
ILE
A
170
1.441
68.804
16.207
1.00
36.57


ATOM
1042
O
ILE
A
170
2.379
68.005
16.315
1.00
36.18


ATOM
1043
CB
ILE
A
170
1.492
70.575
14.461
1.00
34.17


ATOM
1044
CG1
ILE
A
170
1.128
70.944
13.021
1.00
34.33


ATOM
1045
CG2
ILE
A
170
2.997
70.586
14.644
1.00
35.76


ATOM
1046
CD1
ILE
A
170
1.724
72.254
12.572
1.00
38.92


ATOM
1047
N
ALA
A
171
0.866
69.402
17.251
1.00
33.98


ATOM
1049
CA
ALA
A
171
1.308
69.171
18.621
1.00
33.66


ATOM
1049
C
ALA
A
171
1.072
67.731
19.065
1.00
39.36


ATOM
1050
O
ALA
A
171
1.935
67.104
19.675
1.00
39.76


ATOM
1051
CB
ALA
A
171
0.632
70.143
19.562
1.00
34.11


ATOM
1052
N
VAL
A
172
−0.099
67.208
18.766
1.00
35.90


ATOM
1053
CA
VAL
A
172
−0.397
65.849
19.126
1.00
36.13


ATOM
1054
C
VAL
A
172
0.483
64.867
18.348
1.00
42.01


ATOM
1055
O
VAL
A
172
0.997
63.899
18.914
1.00
42.53


ATOM
1056
CB
VAL
A
172
−1.855
65.525
18.897
1.00
39.59


ATOM
1057
CG1
VAL
A
172
−2.117
64.047
19.209
1.00
39.12


ATOM
1058
CG2
VAL
A
172
−2.735
66.438
19.765
1.00
39.46


ATOM
1059
N
ILE
A
173
0.645
65.106
17.051
1.00
38.58


ATOM
1060
CA
ILE
A
173
1.467
64.225
16.244
1.00
38.47


ATOM
1061
C
ILE
A
173
2.900
64.208
16.782
1.00
42.05


ATOM
1062
O
ILE
A
173
3.523
63.153
16.863
1.00
41.56


ATOM
1063
CB
ILE
A
173
1.518
64.657
14.768
1.00
41.34


ATOM
1064
CG1
ILE
A
173
0.201
64.340
14.060
1.00
41.75


ATOM
1065
CG2
ILE
A
173
2.642
63.933
14.062
1.00
42.52


ATOM
1066
CD1
ILE
A
173
0.027
65.078
12.743
1.00
41.85


ATOM
1067
N
LYS
A
174
3.423
65.391
17.104
1.00
38.05


ATOM
1068
CA
LYS
A
174
4.799
65.522
17.574
1.00
37.85


ATOM
1069
C
LYS
A
174
4.983
64.964
18.964
1.00
41.99


ATOM
1070
O
LYS
A
174
6.050
64.465
19.301
1.00
40.88


ATOM
1071
CB
LYS
A
174
5.270
66.971
17.511
1.00
39.44


ATOM
1072
CG
LYS
A
174
5.651
67.425
16.127
1.00
43.97


ATOM
1073
CD
LYS
A
174
6.330
68.788
16.154
1.00
46.42


ATOM
1074
CE
LYS
A
174
6.645
69.256
14.746
1.00
51.29


ATOM
1075
NZ
LYS
A
174
7.311
70.586
14.728
1.00
59.15


ATOM
1076
N
GLY
A
175
3.932
65.045
19.769
1.00
39.80


ATOM
1077
CA
GLY
A
175
3.964
64.519
21.123
1.00
39.81


ATOM
1078
C
GLY
A
175
3.992
62.996
21.065
1.00
44.70


ATOM
1079
O
GLY
A
175
4.784
62.354
21.755
1.00
45.16


ATOM
1080
N
LEU
A
176
3.135
62.424
20.225
1.00
40.60


ATOM
1081
CA
LEU
A
176
3.082
60.974
20.062
1.00
40.41


ATOM
1082
C
LEU
A
176
4.389
60.456
19.459
1.00
46.63


ATOM
1083
O
LEU
A
176
4.830
59.342
19.757
1.00
46.54


ATOM
1084
CB
LEU
A
176
1.917
60.575
19.163
1.00
39.68


ATOM
1085
CG
LEU
A
176
0.502
60.846
19.669
1.00
42.92


ATOM
1086
CD1
LEU
A
176
−0.534
60.500
18.571
1.00
42.64


ATOM
1087
CD2
LEU
A
176
0.236
60.059
20.927
1.00
42.95


ATOM
1088
N
THR
A
177
4.991
61.264
18.598
1.00
44.44


ATOM
1089
CA
THR
A
177
6.232
60.891
17.934
1.00
44.75


ATOM
1090
C
THR
A
177
7.407
60.895
18.898
1.00
49.46


ATOM
1091
O
THR
A
177
8.346
60.120
18.745
1.00
49.49


ATOM
1092
CB
THR
A
177
6.543
61.831
16.770
1.00
54.09


ATOM
1093
OG1
THR
A
177
5.526
61.697
15.765
1.00
55.60


ATOM
1094
CG2
THR
A
177
7.920
61.499
16.161
1.00
51.56


ATOM
1095
N
TYR
A
178
7.353
61.777
19.887
1.00
45.90


ATOM
1096
CA
TYR
A
178
8.419
61.874
20.857
1.00
45.44


ATOM
1097
C
TYR
A
178
8.359
60.690
21.819
1.00
48.84


ATOM
1098
O
TYR
A
178
9.387
60.121
22.188
1.00
48.37


ATOM
1099
CB
TYR
A
178
8.336
63.189
21.631
1.00
46.53


ATOM
1100
CG
TYR
A
178
9.214
63.194
22.861
1.00
48.50


ATOM
1101
CD1
TYR
A
178
8.768
62.650
24.055
1.00
50.65


ATOM
1102
CD2
TYR
A
178
10.518
63.676
22.807
1.00
49.11


ATOM
1103
CE1
TYR
A
178
9.584
62.611
25.175
1.00
52.01


ATOM
1104
CE2
TYR
A
178
11.337
63.650
23.924
1.00
49.79


ATOM
1105
CZ
TYR
A
178
10.867
63.109
25.099
1.00
57.66


ATOM
1106
OH
TYR
A
178
11.675
63.074
26.207
1.00
59.40


ATOM
1107
N
LEU
A
179
7.148
60.316
22.208
1.00
44.58


ATOM
1108
CA
LEU
A
179
6.961
59.196
23.112
1.00
44.57


ATOM
1109
C
LEU
A
179
7.466
57.899
22.497
1.00
51.51


ATOM
1110
O
LEU
A
179
8.054
57.062
23.182
1.00
51.22


ATOM
1111
CB
LEU
A
179
5.492
59.068
23.505
1.00
44.16


ATOM
1112
CG
LEU
A
179
5.010
60.217
24.395
1.00
48.28


ATOM
1113
CD1
LEU
A
179
3.558
60.054
24.769
1.00
48.50


ATOM
1114
CD2
LEU
A
179
5.879
60.333
25.643
1.00
49.44


ATOM
1115
N
ARG
A
180
7.258
57.758
21.193
1.00
50.19


ATOM
1116
CA
ARG
A
180
7.674
56.579
20.455
1.00
50.80


ATOM
1117
C
ARG
A
180
9.191
56.530
20.241
1.00
55.94


ATOM
1118
O
ARG
A
180
9.842
55.535
20.541
1.00
55.50


ATOM
1119
CB
ARG
A
180
6.967
56.552
19.098
1.00
51.86


ATOM
1120
CG
ARG
A
180
6.194
55.271
18.813
1.00
64.13


ATOM
1121
CD
ARG
A
180
6.118
55.017
17.318
1.00
74.72


ATOM
1122
NE
ARG
A
180
6.684
56.129
16.551
1.00
82.23


ATOM
1123
CZ
ARG
A
180
6.983
56.070
15.257
1.00
94.42


ATOM
1124
NH1
ARG
A
180
6.771
54.947
14.576
1.00
82.23


ATOM
1125
NH2
ARG
A
180
7.502
57.129
14.643
1.00
75.18


ATOM
1126
N
GLU
A
181
9.735
57.605
19.691
1.00
53.47


ATOM
1127
CA
GLU
A
181
11.155
57.678
19.379
1.00
53.56


ATOM
1128
C
GLU
A
181
12.056
57.605
20.599
1.00
57.26


ATOM
1129
O
GLU
A
181
12.979
56.790
20.650
1.00
57.08


ATOM
1130
CB
GLU
A
181
11.462
58.956
18.595
1.00
55.10


ATOM
1131
CG
GLU
A
181
10.841
58.992
17.223
1.00
68.50


ATOM
1132
CD
GLU
A
181
11.153
57.744
16.419
1.00
96.65


ATOM
1133
OE1
GLU
A
181
10.219
56.951
16.159
1.00
94.99


ATOM
1134
OE2
GLU
A
181
12.339
57.546
16.068
1.00
91.47


ATOM
1135
N
LYS
A
182
11.820
58.496
21.558
1.00
52.84


ATOM
1136
CA
LYS
A
182
12.669
58.588
22.735
1.00
51.94


ATOM
1137
C
LYS
A
182
12.386
57.602
23.849
1.00
55.47


ATOM
1138
O
LYS
A
182
13.267
57.316
24.654
1.00
55.55


ATOM
1139
CB
LYS
A
182
12.673
60.014
23.281
1.00
54.15


ATOM
1140
CG
LYS
A
182
13.076
61.069
22.256
1.00
66.05


ATOM
1141
CD
LYS
A
182
14.505
60.862
21.799
1.00
77.82


ATOM
1142
CE
LYS
A
182
14.933
61.932
20.807
1.00
93.36


ATOM
1143
NZ
LYS
A
182
16.410
61.920
20.575
1.00
103.78


ATOM
1144
N
HIS
A
183
11.166
57.090
23.921
1.00
51.26


ATOM
1145
CA
HIS
A
183
10.816
56.195
25.016
1.00
50.74


ATOM
1146
C
HIS
A
183
10.124
54.914
24.593
1.00
54.31


ATOM
1147
O
HIS
A
183
9.774
54.083
25.438
1.00
52.81


ATOM
1148
CB
HIS
A
183
9.982
56.954
26.078
1.00
51.49


ATOM
1149
CG
HIS
A
183
10.568
58.276
26.463
1.00
54.72


ATOM
1150
ND1
HIS
A
183
11.507
58.408
27.462
1.00
56.46


ATOM
1151
CD2
HIS
A
183
10.407
59.511
25.933
1.00
56.55


ATOM
1152
CE1
HIS
A
183
11.879
59.673
27.552
1.00
55.92


ATOM
1153
NE2
HIS
A
183
11.232
60.363
26.631
1.00
56.37


ATOM
1154
N
LYS
A
184
9.953
54.748
23.286
1.00
52.04


ATOM
1155
CA
LYS
A
184
9.317
53.559
22.729
1.00
52.76


ATOM
1156
C
LYS
A
184
8.036
53.234
23.451
1.00
57.54


ATOM
1157
O
LYS
A
184
7.830
52.106
23.893
1.00
57.28


ATOM
1158
CB
LYS
A
184
10.265
52.351
22.769
1.00
55.87


ATOM
1159
CG
LYS
A
184
11.390
52.405
21.734
1.00
74.74


ATOM
1160
CD
LYS
A
184
12.149
51.079
21.660
1.00
88.25


ATOM
1161
CE
LYS
A
184
13.174
51.075
20.517
1.00
101.72


ATOM
1162
NZ
LYS
A
184
13.294
49.735
19.851
1.00
109.61


ATOM
1163
N
ILE
A
185
7.185
54.240
23.599
1.00
54.52


ATOM
1164
CA
ILE
A
185
5.896
54.056
24.235
1.00
53.95


ATOM
1165
C
ILE
A
185
4.810
54.856
23.540
1.00
55.99


ATOM
1166
O
ILE
A
185
5.096
55.763
22.762
1.00
55.11


ATOM
1167
CB
ILE
A
185
5.934
54.349
25.724
1.00
57.27


ATOM
1168
CG1
ILE
A
185
6.385
55.787
25.987
1.00
57.67


ATOM
1169
CG2
ILE
A
185
6.837
53.338
26.433
1.00
58.37


ATOM
1170
CD1
ILE
A
185
6.509
56.121
27.474
1.00
61.27


ATOM
1171
N
MET
A
186
3.566
54.463
23.767
1.00
51.75


ATOM
1172
CA
MET
A
186
2.444
55.114
23.133
1.00
51.03


ATOM
1173
C
MET
A
186
1.546
55.707
24.182
1.00
50.78


ATOM
1174
O
MET
A
186
1.620
55.336
25.347
1.00
50.76


ATOM
1175
CB
MET
A
186
1.679
54.129
22.263
1.00
54.00


ATOM
1176
CG
MET
A
186
0.824
53.163
23.023
1.00
58.35


ATOM
1177
SD
MET
A
186
−0.026
52.048
21.890
1.00
63.39


ATOM
1178
CE
MET
A
186
−1.755
52.756
21.961
1.00
59.99


ATOM
1179
N
HIS
A
187
0.720
56.662
23.784
1.00
43.67


ATOM
1180
CA
HIS
A
187
−0.151
57.324
24.745
1.00
41.38


ATOM
1181
C
HIS
A
187
−1.201
56.399
25.340
1.00
43.50


ATOM
1182
0
HIS
A
187
−1.254
56.221
26.554
1.00
42.07


ATOM
1183
CB
HIS
A
187
−0.810
58.573
24.137
1.00
40.80


ATOM
1184
CG
HIS
A
187
−1.328
59.532
25.160
1.00
43.03


ATOM
1185
ND1
HIS
A
187
−2.457
59.278
25.911
1.00
44.18


ATOM
1186
CD2
HIS
A
187
−0.854
60.728
25.584
1.00
43.71


ATOM
1187
CE1
HIS
A
187
−2.672
60.292
26.731
1.00
43.16


ATOM
1188
NE2
HIS
A
187
−1.707
61.179
26.560
1.00
43.37


ATOM
1189
N
ARG
A
188
−2.058
55.851
24.474
1.00
39.74


ATOM
1190
CA
ARG
A
188
−3.140
54.936
24.874
1.00
39.28


ATOM
1191
C
ARG
A
188
−4.388
55.631
25.366
1.00
42.30


ATOM
1192
O
ARG
A
188
−5.429
55.012
25.506
1.00
42.44


ATOM
1193
CB
ARG
A
188
−2.666
53.900
25.897
1.00
40.21


ATOM
1194
CG
ARG
A
188
−2.047
52.661
25.274
1.00
54.29


ATOM
1195
CD
ARG
A
188
−1.717
51.613
26.330
1.00
68.54


ATOM
1196
NE
ARG
A
188
−0.278
51.403
26.450
1.00
79.47


ATOM
1197
CZ
ARG
A
188
0.365
50.346
25.968
1.00
93.79


ATOM
1198
NH1
ARG
A
188
−0.304
49.391
25.335
1.00
79.39


ATOM
1199
NH2
ARG
A
188
1.678
50.245
26.120
1.00
82.59


ATOM
1200
N
ASP
A
189
−4.292
56.922
25.637
1.00
38.34


ATOM
1201
CA
ASP
A
189
−5.459
57.656
26.099
1.00
37.54


ATOM
1202
C
ASP
A
189
−5.509
59.071
25.556
1.00
40.79


ATOM
1203
O
ASP
A
189
−5.529
60.038
26.305
1.00
40.71


ATOM
1204
CB
ASP
A
189
−5.572
57.637
27.621
1.00
38.75


ATOM
1205
CG
ASP
A
189
−6.984
57.966
28.107
1.00
46.14


ATOM
1206
OD1
ASP
A
189
−7.948
57.794
27.320
1.00
44.96


ATOM
1207
OD2
ASP
A
189
−7.126
58.416
29.268
1.00
53.43


ATOM
1208
N
VAL
A
190
−5.533
59.178
24.240
1.00
36.21


ATOM
1209
CA
VAL
A
190
−5.641
60.453
23.594
1.00
35.11


ATOM
1210
C
VAL
A
190
−7.122
60.842
23.543
1.00
39.05


ATOM
1211
O
VAL
A
190
−7.975
60.055
23.117
1.00
38.07


ATOM
1212
CB
VAL
A
190
−5.073
60.401
22.152
1.00
38.44


ATOM
1213
CG1
VAL
A
190
−5.496
61.631
21.364
1.00
37.82


ATOM
1214
CG2
VAL
A
190
−3.544
60.259
22.177
1.00
38.12


ATOM
1215
N
LYS
A
191
−7.418
62.038
24.041
1.00
35.76


ATOM
1216
CA
LYS
A
191
−8.763
62.587
24.038
1.00
35.10


ATOM
1217
C
LYS
A
191
−8.616
64.061
24.394
1.00
38.95


ATOM
1218
O
LYS
A
191
−7.520
64.500
24.706
1.00
38.58


ATOM
1219
CB
LYS
A
191
−9.656
61.846
25.025
1.00
37.08


ATOM
1220
CG
LYS
A
191
−9.263
62.004
26.472
1.00
39.86


ATOM
1221
CD
LYS
A
191
−10.073
61.074
27.336
1.00
41.76


ATOM
1222
CE
LYS
A
191
−9.474
60.929
28.721
1.00
45.17


ATOM
1223
NZ
LYS
A
191
−10.442
60.299
29.654
1.00
49.49


ATOM
1224
N
PRO
A
192
−9.694
64.835
24.300
1.00
35.63


ATOM
1225
CA
PRO
A
192
−9.599
66.296
24.525
1.00
35.49


ATOM
1226
C
PRO
A
192
−9.132
66.751
25.907
1.00
40.27


ATOM
1227
O
PRO
A
192
−8.425
67.753
26.031
1.00
40.46


ATOM
1228
CB
PRO
A
192
−11.018
66.800
24.211
1.00
36.75


ATOM
1229
CG
PRO
A
192
−11.546
65.806
23.200
1.00
40.38


ATOM
1230
CD
PRO
A
192
−10.950
64.458
23.612
1.00
35.78


ATOM
1231
N
SER
A
193
−9.502
66.005
26.939
1.00
36.70


ATOM
1232
CA
SER
A
193
−9.121
66.351
28.302
1.00
36.00


ATOM
1233
C
SER
A
193
−7.660
66.039
28.583
1.00
40.44


ATOM
1234
O
SER
A
193
−7.134
66.399
29.643
1.00
39.99


ATOM
1235
CB
SER
A
193
−10.008
65.612
29.307
1.00
38.52


ATOM
1236
OG
SER
A
193
−9.756
64.217
29.272
1.00
44.18


ATOM
1237
N
ASN
A
194
−7.012
65.339
27.651
1.00
36.67


ATOM
1238
CA
ASN
A
194
−5.606
64.972
27.818
1.00
35.83


ATOM
1239
C
ASN
A
194
−4.710
65.803
26.952
1.00
38.88


ATOM
1240
O
ASN
A
194
−3.531
65.495
26.784
1.00
39.15


ATOM
1241
CB
ASN
A
194
−5.377
63.481
27.577
1.00
34.06


ATOM
1242
CG
ASN
A
194
−5.727
62.651
28.778
1.00
49.75


ATOM
1243
OD1
ASN
A
194
−5.897
63.181
29.875
1.00
39.18


ATOM
1244
ND2
ASN
A
194
−5.893
61.345
28.576
1.00
43.31


ATOM
1245
N
ILE
A
195
−5.278
66.859
26.388
1.00
34.44


ATOM
1246
CA
ILE
A
195
−4.507
67.824
25.621
1.00
33.70


ATOM
1247
C
ILE
A
195
−4.605
69.153
26.362
1.00
38.37


ATOM
1248
O
ILE
A
195
−5.671
69.756
26.441
1.00
37.24


ATOM
1249
CB
ILE
A
195
−5.003
67.966
24.173
1.00
35.80


ATOM
1250
CG1
ILE
A
195
−5.068
66.585
23.501
1.00
36.08


ATOM
1251
CG2
ILE
A
195
−4.053
68.880
23.366
1.00
34.47


ATOM
1252
CD1
ILE
A
195
−5.987
66.532
22.279
1.00
37.39


ATOM
1253
N
LEU
A
196
−3.504
69.546
26.995
1.00
35.79


ATOM
1254
CA
LEU
A
196
−3.471
70.777
27.779
1.00
34.99


ATOM
1255
C
LEU
A
196
−2.859
71.915
27.002
1.00
36.56


ATOM
1256
O
LEU
A
196
−1.996
71.707
26.162
1.00
35.75


ATOM
1257
CB
LEU
A
196
−2.726
70.558
29.089
1.00
35.09


ATOM
1258
CG
LEU
A
196
−3.200
69.335
29.889
1.00
39.73


ATOM
1259
CD1
LEU
A
196
−2.390
69.165
31.186
1.00
40.14


ATOM
1260
CD2
LEU
A
196
−4.690
69.396
30.172
1.00
39.68


ATOM
1261
N
VAL
A
197
−3.345
73.123
27.258
1.00
32.19


ATOM
1262
CA
VAL
A
197
−2.864
74.317
26.559
1.00
31.10


ATOM
1263
C
VAL
A
197
−2.581
75.445
27.546
1.00
32.95


ATOM
1264
O
VAL
A
197
−3.055
75.421
28.674
1.00
31.09


ATOM
1265
CB
VAL
A
197
−3.885
74.794
25.464
1.00
34.46


ATOM
1266
CG1
VAL
A
197
−3.906
73.805
24.298
1.00
34.31


ATOM
1267
CG2
VAL
A
197
−5.282
74.942
26.049
1.00
33.84


ATOM
1268
N
ASN
A
198
−1.768
76.409
27.134
1.00
30.55


ATOM
1269
CA
ASN
A
198
−1.422
77.518
28.030
1.00
30.82


ATOM
1270
C
ASN
A
198
−1.370
78.897
27.356
1.00
36.36


ATOM
1271
O
ASN
A
198
−1.386
79.003
26.127
1.00
34.55


ATOM
1272
CB
ASN
A
198
−0.149
77.214
28.861
1.00
26.74


ATOM
1273
CG
ASN
A
198
1.133
77.258
28.032
1.00
42.92


ATOM
1274
OD1
ASN
A
198
1.182
77.855
26.945
1.00
33.94


ATOM
1275
ND2
ASN
A
198
2.188
76.640
28.557
1.00
33.50


ATOM
1276
N
SER
A
199
−1.358
79.947
28.176
1.00
35.32


ATOM
1277
CA
SER
A
199
−1.336
81.318
27.671
1.00
36.15


ATOM
1278
C
SER
A
199
−0.093
81.630
26.825
1.00
42.22


ATOM
1279
O
SER
A
199
−0.059
82.626
26.112
1.00
42.44


ATOM
1280
CB
SER
A
199
−1.474
82.325
28.816
1.00
39.30


ATOM
1281
OG
SER
A
199
−0.458
82.144
29.770
1.00
45.77


ATOM
1282
N
ARG
A
200
0.915
80.766
26.881
1.00
39.72


ATOM
1283
CA
ARG
A
200
2.103
80.970
26.048
1.00
40.59


ATOM
1284
C
ARG
A
200
1.876
80.426
24.623
1.00
45.58


ATOM
1285
O
ARG
A
200
2.664
80.686
23.715
1.00
45.25


ATOM
1286
CB
ARG
A
200
3.342
80.330
26.682
1.00
42.16


ATOM
1287
CG
ARG
A
200
3.955
81.157
27.794
1.00
55.01


ATOM
1288
CD
ARG
A
200
4.828
80.309
28.701
1.00
70.71


ATOM
1289
NE
ARG
A
200
5.991
81.050
29.178
1.00
85.95


ATOM
1290
CZ
ARG
A
200
7.228
80.566
29.204
1.00
102.21


ATOM
1291
NH1
ARG
A
200
7.468
79.335
28.767
1.00
86.36


ATOM
1292
NH2
ARG
A
200
8.229
81.319
29.651
1.00
92.86


ATOM
1293
N
GLY
A
201
0.788
79.670
24.440
1.00
41.85


ATOM
1294
CA
GLY
A
201
0.454
79.122
23.128
1.00
41.23


ATOM
1295
C
GLY
A
201
0.986
77.706
22.960
1.00
43.37


ATOM
1296
O
GLY
A
201
1.135
77.210
21.843
1.00
43.04


ATOM
1297
N
GLU
A
202
1.296
77.072
24.075
1.00
38.20


ATOM
1298
CA
GLU
A
202
1.815
75.725
24.044
1.00
37.06


ATOM
1299
C
GLU
A
202
0.685
74.717
24.123
1.00
39.35


ATOM
1300
O
GLU
A
202
−0.308
74.935
24.810
1.00
37.90


ATOM
1301
CB
GLU
A
202
2.800
75.498
25.189
1.00
38.07


ATOM
1302
CG
GLU
A
202
4.014
76.414
25.146
1.00
45.19


ATOM
1303
CD
GLU
A
202
4.947
76.205
26.331
1.00
60.89


ATOM
1304
OE1
GLU
A
202
4.477
76.290
27.493
1.00
44.79


ATOM
1305
OE2
GLU
A
202
6.146
75.938
26.102
1.00
52.24


ATOM
1306
N
ILE
A
203
0.856
73.613
23.404
1.00
35.00


ATOM
1307
CA
ILE
A
203
−0.106
72.530
23.389
1.00
34.27


ATOM
1308
C
ILE
A
203
0.664
71.276
23.773
1.00
37.30


ATOM
1309
O
ILE
A
203
1.731
71.026
23.235
1.00
36.05


ATOM
1310
CB
ILE
A
203
−0.749
72.387
21.984
1.00
36.90


ATOM
1311
CG1
ILE
A
203
−1.302
73.755
21.529
1.00
36.68


ATOM
1312
CG2
ILE
A
203
−1.876
71.343
22.018
1.00
36.43


ATOM
1313
CD1
ILE
A
203
−1.175
74.026
20.055
1.00
37.04


ATOM
1314
N
LYS
A
204
0.174
70.546
24.778
1.00
33.74


ATOM
1315
CA
LYS
A
204
0.910
69.396
25.304
1.00
33.36


ATOM
1316
C
LYS
A
204
0.049
68.226
25.700
1.00
38.05


ATOM
1317
O
LYS
A
204
−1.080
68.391
26.152
1.00
38.40


ATOM
1318
CB
LYS
A
204
1.758
69.811
26.515
1.00
34.67


ATOM
1319
CG
LYS
A
204
2.686
70.990
26.254
1.00
37.25


ATOM
1320
CD
LYS
A
204
3.461
71.377
27.507
1.00
34.93


ATOM
1321
CE
LYS
A
204
4.548
72.392
27.186
1.00
38.52


ATOM
1322
NZ
LYS
A
204
5.350
72.781
28.390
1.00
41.91


ATOM
1323
N
LEU
A
205
0.605
67.030
25.569
1.00
34.62


ATOM
1324
CA
LEU
A
205
−0.108
65.835
25.976
1.00
34.60


ATOM
1325
C
LEU
A
205
0.190
65.491
27.437
1.00
39.53


ATOM
1326
O
LEU
A
205
1.282
65.770
27.959
1.00
38.81


ATOM
1327
CB
LEU
A
205
0.284
64.659
25.095
1.00
34.42


ATOM
1328
CG
LEU
A
205
0.069
64.842
23.603
1.00
38.35


ATOM
1329
CD1
LEU
A
205
0.864
63.785
22.835
1.00
38.40


ATOM
1330
CD2
LEU
A
205
−1.392
64.753
23.292
1.00
38.38


ATOM
1331
N
CYS
A
206
−0.770
64.857
28.084
1.00
37.38


ATOM
1332
CA
CYS
A
206
−0.579
64.409
29.451
1.00
37.86


ATOM
1333
C
CYS
A
206
−1.308
63.097
29.645
1.00
42.78


ATOM
1334
O
CYS
A
206
−2.101
62.684
28.798
1.00
41.19


ATOM
1335
CB
CYS
A
206
−1.116
65.446
30.439
1.00
38.31


ATOM
1336
SG
CYS
A
206
−2.932
65.599
30.439
1.00
42.22


ATOM
1337
N
ASP
A
207
−1.042
62.450
30.773
1.00
41.70


ATOM
1338
CA
ASP
A
207
−1.739
61.226
31.149
1.00
42.72


ATOM
1339
C
ASP
A
207
−1.559
60.015
30.247
1.00
49.53


ATOM
1340
O
ASP
A
207
−2.523
59.335
29.926
1.00
47.22


ATOM
1341
CB
ASP
A
207
−3.223
61.497
31.378
1.00
44.71


ATOM
1342
CG
ASP
A
207
−3.491
62.204
32.698
1.00
54.89


ATOM
1343
OD1
ASP
A
207
−2.615
62.179
33.576
1.00
55.15


ATOM
1344
OD2
ASP
A
207
−4.573
62.810
32.843
1.00
63.16


ATOM
1345
N
PHE
A
208
−0.315
59.728
29.869
1.00
51.05


ATOM
1346
CA
PHE
A
208
−0.002
58.511
29.126
1.00
53.13


ATOM
1347
C
PHE
A
208
0.421
57.496
30.195
1.00
61.97


ATOM
1348
O
PHE
A
208
1.269
57.788
31.033
1.00
62.56


ATOM
1349
CB
PHE
A
208
1.134
58.742
28.118
1.00
54.93


ATOM
1350
CG
PHE
A
208
2.103
59.812
28.524
1.00
56.63


ATOM
1351
CD1
PHE
A
208
3.288
59.489
29.171
1.00
59.79


ATOM
1352
CD2
PHE
A
208
1.826
61.143
28.267
1.00
58.58


ATOM
1353
CE1
PHE
A
208
4.176
60.477
29.552
1.00
60.55


ATOM
1354
CE2
PHE
A
208
2.706
62.132
28.641
1.00
61.34


ATOM
1355
CZ
PHE
A
208
3.882
61.802
29.290
1.00
59.46


ATOM
1356
N
GLY
A
209
−0.219
56.331
30.206
1.00
61.60


ATOM
1357
CA
GLY
A
209
0.043
55.314
31.228
1.00
62.70


ATOM
1358
C
GLY
A
209
1.453
54.720
31.212
1.00
69.58


ATOM
1359
O
GLY
A
209
1.717
53.752
30.501
1.00
70.24


ATOM
1360
N
VAL
A
210
2.340
55.271
32.040
1.00
66.94


ATOM
1361
CA
VAL
A
210
3.699
54.762
32.133
1.00
67.15


ATOM
1362
C
VAL
A
210
3.841
53.718
33.253
1.00
71.97


ATOM
1363
O
VAL
A
210
4.849
53.018
33.338
1.00
71.18


ATOM
1364
CB
VAL
A
210
4.720
55.899
32.344
1.00
71.15


ATOM
1365
CG1
VAL
A
210
6.133
55.346
32.377
1.00
71.06


ATOM
1366
CG2
VAL
A
210
4.583
56.943
31.257
1.00
70.92


ATOM
1367
N
SER
A
211
2.827
53.618
34.104
1.00
69.66


ATOM
1368
CA
SER
A
211
2.851
52.668
35.216
1.00
69.96


ATOM
1369
C
SER
A
211
1.743
51.603
35.112
1.00
74.88


ATOM
1370
O
SER
A
211
0.554
51.920
35.158
1.00
73.71


ATOM
1371
CB
SER
A
211
2.715
53.412
36.548
1.00
73.35


ATOM
1372
OG
SER
A
211
1.892
52.697
37.461
1.00
80.46


ATOM
1373
N
GLY
A
212
2.141
50.343
34.991
1.00
73.07


ATOM
1374
CA
GLY
A
212
1.184
49.239
34.892
1.00
73.68


ATOM
1375
C
GLY
A
212
0.421
49.041
36.205
1.00
79.25


ATOM
1376
O
GLY
A
212
−0.783
48.778
36.199
1.00
78.59


ATOM
1377
N
GLN
A
213
1.107
49.178
37.322
1.00
77.27


ATOM
1378
CA
GLN
A
213
0.462
49.014
38.613
1.00
78.06


ATOM
1379
C
GLN
A
213
−0.689
49.996
38.829
1.00
83.84


ATOM
1380
O
GLN
A
213
−1.798
49.591
39.134
1.00
83.37


ATOM
1381
CB
GLN
A
213
1.489
49.155
39.740
1.00
79.49


ATOM
1382
CG
GLN
A
213
1.426
48.031
40.769
1.00
94.29


ATOM
1383
CD
GLN
A
213
0.075
47.263
40.817
1.00
111.26


ATOM
1384
OE2
GLN
A
213
−0.974
47.868
40.763
1.00
106.71


ATOM
1385
NE2
GLN
A
213
0.168
45.964
41.000
1.00
102.06


ATOM
1386
N
LEU
A
214
−0.402
51.290
38.696
1.00
81.71


ATOM
1387
CA
LEU
A
214
−1.421
52.308
38.872
1.00
82.09


ATOM
1388
C
LEU
A
214
−2.603
52.002
37.961
1.00
86.86


ATOM
1389
O
LEU
A
214
−3.766
52.244
38.310
1.00
86.30


ATOM
1390
CB
LEU
A
214
−0.852
53.695
38.563
1.00
82.11


ATOM
1391
CG
LEU
A
214
−1.827
54.860
38.609
1.00
86.64


ATOM
1392
CD1
LEU
A
214
−2.500
54.936
39.974
1.00
86.71


ATOM
1393
CD2
LEU
A
214
−1.085
56.150
38.298
1.00
88.48


ATOM
1394
N
ILE
A
215
−2.295
51.461
36.793
1.00
83.92


ATOM
1395
CA
ILE
A
215
−3.321
51.097
35.838
1.00
83.90


ATOM
1396
C
ILE
A
215
−4.213
50.005
36.447
1.00
85.96


ATOM
1397
O
ILE
A
215
−5.433
50.166
36.550
1.00
85.39


ATOM
1398
CB
ILE
A
215
−2.714
50.594
34.509
1.00
87.41


ATOM
1399
CG1
ILE
A
215
−2.456
51.772
33.559
1.00
87.96


ATOM
1400
CG2
ILE
A
215
−3.643
49.573
33.861
1.00
88.24


ATOM
1401
CD1
ILE
A
215
−1.685
51.402
32.301
1.00
94.18


ATOM
1402
N
ASP
A
216
−3.585
48.925
36.898
1.00
81.24


ATOM
1403
CA
ASP
A
216
−4.313
47.817
37.499
1.00
80.65


ATOM
1404
C
ASP
A
216
−5.136
48.239
38.720
1.00
84.01


ATOM
1405
O
ASP
A
216
−6.360
48.092
38.734
1.00
83.92


ATOM
1406
CB
ASP
A
216
−3.361
46.678
37.875
1.00
82.34


ATOM
1407
CG
ASP
A
216
−2.722
46.034
36.671
1.00
91.15


ATOM
1408
OD1
ASP
A
216
−3.262
46.187
35.555
1.00
91.28


ATOM
1409
OD2
ASP
A
216
−1.659
45.398
36.835
1.00
97.72


ATOM
1410
N
SER
A
217
−4.457
48.733
39.751
1.00
79.51


ATOM
1411
CA
SER
A
217
−5.117
49.155
40.980
1.00
78.83


ATOM
1412
C
SER
A
217
−6.279
50.099
40.720
1.00
82.02


ATOM
1413
O
SER
A
217
−7.233
50.155
41.503
1.00
81.70


ATOM
1414
CB
SER
A
217
−4.114
49.805
41.925
1.00
82.55


ATOM
1415
OG
SER
A
217
−2.790
49.609
41.466
1.00
92.39


ATOM
1416
N
MET
A
218
−6.191
50.853
39.631
1.00
79.24


ATOM
1417
CA
MET
A
218
−7.245
51.789
39.264
1.00
78.96


ATOM
1418
C
MET
A
218
−8.324
51.091
38.445
1.00
83.42


ATOM
1419
O
MET
A
218
−9.453
51.565
38.376
1.00
84.11


ATOM
1420
CB
MET
A
218
−6.669
52.962
38.474
1.00
81.30


ATOM
1421
CG
MET
A
218
−5.932
53.977
39.319
1.00
84.76


ATOM
1422
SD
MET
A
218
−5.612
55.521
38.424
1.00
89.07


ATOM
1423
CE
MET
A
218
−5.015
54.881
36.820
1.00
85.46


ATOM
1424
N
ALA
A
219
−7.958
49.971
37.822
1.00
82.00


ATOM
1425
CA
ALA
A
219
−8.890
49.195
37.013
1.00
83.34


ATOM
1426
C
ALA
A
219
−10.133
48.923
37.840
1.00
88.71


ATOM
1427
O
ALA
A
219
−11.240
48.796
37.308
1.00
89.06


ATOM
1428
CB
ALA
A
219
−8.246
47.881
36.578
1.00
84.05


ATOM
1429
N
ASN
A
220
−9.947
48.876
39.150
1.00
86.94


ATOM
1430
CA
ASN
A
220
−11.041
48.636
40.068
1.00
86.90


ATOM
1431
C
ASN
A
220
−12.134
49.686
39.892
1.00
89.45


ATOM
1432
O
ASN
A
220
−13.018
49.538
39.041
1.00
89.85


ATOM
1433
CB
ASN
A
220
−10.524
48.625
41.506
1.00
89.25


ATOM
1434
CG
ASN
A
220
−9.337
47.710
41.684
1.00
117.91


ATOM
1435
OD1
ASN
A
220
−9.322
46.595
41.175
1.00
113.07


ATOM
1436
ND2
ASN
A
220
−8.309
48.201
42.361
1.00
111.67


ATOM
1437
N
SER
A
221
−12.062
50.754
40.675
1.00
84.14


ATOM
1438
CA
SER
A
221
−13.069
51.810
40.609
1.00
83.64


ATOM
1439
C
SER
A
221
−12.594
53.059
39.862
1.00
86.58


ATOM
1440
O
SER
A
221
−13.070
54.172
40.132
1.00
86.17


ATOM
1441
CB
SER
A
221
−13.504
52.197
42.019
1.00
87.91


ATOM
1442
OG
SER
A
221
−12.527
53.014
42.643
1.00
98.28


ATOM
1443
N
PHE
A
222
−11.671
52.891
38.921
1.00
81.11


ATOM
1444
CA
PHE
A
222
−11.132
54.043
38.193
1.00
80.24


ATOM
1445
C
PHE
A
222
−11.152
53.900
36.665
1.00
80.45


ATOM
1446
O
PHE
A
222
−10.166
54.226
36.007
1.00
79.28


ATOM
1447
CB
PHE
A
222
−9.690
54.338
38.645
1.00
82.59


ATOM
1448
CG
PHE
A
222
−9.526
54.471
40.138
1.00
85.09


ATOM
1449
CD1
PHE
A
222
−9.868
53.424
40.985
1.00
87.79


ATOM
1450
CD2
PHE
A
222
−8.964
55.627
40.685
1.00
87.17


ATOM
1451
CE1
PHE
A
222
−9.704
53.549
42.356
1.00
88.39


ATOM
1452
CE2
PHE
A
222
−8.791
55.743
42.057
1.00
89.66


ATOM
1453
CZ
PHE
A
222
−9.197
54.721
42.890
1.00
87.51


ATOM
1454
N
VAL
A
223
−12.273
53.458
36.098
1.00
71.87


ATOM
1455
CA
VAL
A
223
−12.356
53.291
34.643
1.00
69.31


ATOM
1456
C
VAL
A
223
−12.752
54.583
33.896
1.00
67.93


ATOM
1457
O
VAL
A
223
−13.813
55.158
34.156
1.00
68.30


ATOM
1458
CB
VAL
A
223
−13.303
52.131
34.251
1.00
73.25


ATOM
1459
CG1
VAL
A
223
−14.626
52.229
35.013
1.00
72.69


ATOM
1460
CG2
VAL
A
223
−13.533
52.103
32.741
1.00
72.72


ATOM
1461
N
GLY
A
224
−11.883
55.034
32.986
1.00
59.03


ATOM
1462
CA
GLY
A
224
−12.129
56.247
32.191
1.00
56.95


ATOM
1463
C
GLY
A
224
−12.777
55.891
30.845
1.00
56.73


ATOM
1464
O
GLY
A
224
−12.635
54.769
30.366
1.00
56.41


ATOM
1465
N
THR
A
224
−13.482
56.858
30.245
1.00
49.18


ATOM
1466
CA
THR
A
225
−14.209
56.642
28.984
1.00
47.11


ATOM
1467
C
THR
A
225
−13.484
55.869
27.882
1.00
47.60


ATOM
1468
O
THR
A
225
−12.316
56.124
27.586
1.00
46.57


ATOM
1469
CB
THR
A
225
−14.781
57.964
28.396
1.00
55.36


ATOM
1470
OG1
THR
A
225
−15.895
57.661
27.549
1.00
58.96


ATOM
1471
CG2
THR
A
225
−13.729
58.681
27.567
1.00
52.02


ATOM
1472
N
ARG
A
226
−14.227
54.973
27.230
1.00
42.60


ATOM
1473
CA
ARG
A
226
−13.722
54.172
26.109
1.00
40.95


ATOM
1474
C
ARG
A
226
−14.221
54.754
24.779
1.00
41.00


ATOM
1475
O
ARG
A
226
−13.918
54.236
23.704
1.00
39.24


ATOM
1476
CB
ARG
A
226
−14.222
52.730
26.229
1.00
40.03


ATOM
1477
CG
ARG
A
226
−13.989
52.080
27.595
1.00
47.31


ATOM
1478
CD
ARG
A
226
−13.941
50.533
27.473
1.00
50.43


ATOM
1479
NE
ARG
A
226
−12.580
50.032
27.641
1.00
52.95


ATOM
1480
CZ
ARG
A
226
−12.023
49.090
26.892
1.00
58.66


ATOM
1481
NH1
ARG
A
226
−12.717
48.503
25.918
1.00
37.20


ATOM
1482
NH2
ARG
A
226
−10.771
48.723
27.127
1.00
43.54


ATOM
1483
N
SER
A
227
−14.990
55.825
24.871
1.00
37.40


ATOM
1484
CA
SER
A
227
−15.587
56.468
23.694
1.00
37.40


ATOM
1485
C
SER
A
227
−14.601
57.030
22.673
1.00
40.32


ATOM
1486
O
SER
A
227
−14.993
57.353
21.553
1.00
39.19


ATOM
1487
CB
SER
A
227
−16.607
57.532
24.110
1.00
41.19


ATOM
1488
OG
SER
A
227
−15.995
58.553
24.874
1.00
52.23


ATOM
1489
N
TYR
A
228
−13.317
57.092
23.031
1.00
36.99


ATOM
1490
CA
TYR
A
228
−12.287
57.583
22.091
1.00
36.61


ATOM
1491
C
TYR
A
228
−11.367
56.472
21.586
1.00
44.51


ATOM
1492
O
TYR
A
228
−10.416
56.726
20.821
1.00
44.33


ATOM
1493
CB
TYR
A
228
−11.473
58.706
22.733
1.00
36.39


ATOM
1494
CG
TYR
A
228
−12.290
59.966
22.959
1.00
35.70


ATOM
1495
CD1
TYR
A
228
−12.542
60.846
21.921
1.00
37.18


ATOM
1496
CD2
TYR
A
228
−12.904
60.199
24.178
1.00
35.42


ATOM
1497
CE1
TYR
A
228
−13.319
61.963
22.105
1.00
37.81


ATOM
1498
CE2
TYR
A
228
−13.667
61.326
24.376
1.00
35.97


ATOM
1499
CZ
TYR
A
228
−13.880
62.205
23.341
1.00
42.38


ATOM
1500
OH
TYR
A
228
−14.640
63.332
23.531
1.00
40.08


ATOM
1501
N
MET
A
229
−11.654
55.240
22.005
1.00
42.62


ATOM
1502
CA
MET
A
229
−10.864
54.081
21.606
1.00
42.98


ATOM
1503
C
MET
A
229
−11.124
53.691
20.158
1.00
44.97


ATOM
1504
O
MET
A
229
−12.253
53.751
19.677
1.00
44.57


ATOM
1505
CB
MET
A
229
−11.180
52.892
22.516
1.00
46.06


ATOM
1506
CG
MET
A
229
−10.763
53.102
23.960
1.00
50.65


ATOM
1507
SD
MET
A
229
−10.269
51.572
24.757
1.00
55.63


ATOM
1508
CE
MET
A
229
−9.624
52.201
26.290
1.00
52.52


ATOM
1509
N
SER
A
230
−10.085
53.253
19.476
1.00
40.58


ATOM
1510
CA
SER
A
230
−10.234
52.834
18.095
1.00
40.72


ATOM
1511
C
SER
A
230
−11.036
51.550
18.048
1.00
45.77


ATOM
1512
O
SER
A
230
−11.236
50.898
19.067
1.00
45.93


ATOM
1513
CB
SER
A
230
−8.865
52.619
17.455
1.00
43.20


ATOM
1514
OG
SER
A
230
−8.109
51.684
18.198
1.00
47.73


ATOM
1515
N
PRO
A
231
−11.483
51.178
16.859
1.00
43.15


ATOM
1516
CA
PRO
A
231
−12.258
49.943
16.682
1.00
42.57


ATOM
1517
C
PRO
A
231
−11.425
48.701
17.029
1.00
46.28


ATOM
1518
O
PRO
A
231
−11.893
47.811
17.725
1.00
44.99


ATOM
1519
CB
PRO
A
231
−12.593
49.949
15.182
1.00
43.65


ATOM
1520
CG
PRO
A
231
−12.464
51.367
14.766
1.00
48.11


ATOM
1521
CD
PRO
A
231
−11.366
51.939
15.606
1.00
43.61


ATOM
1522
N
GLU
A
232
−10.185
48.657
16.549
1.00
43.93


ATOM
1523
CA
GLU
A
232
−9.323
47.504
16.801
1.00
44.64


ATOM
1524
C
GLU
A
232
−9.033
47.278
18.290
1.00
52.24


ATOM
1525
O
GLU
A
232
−8.895
46.138
18.732
1.00
52.92


ATOM
1526
CB
GLU
A
232
−8.030
47.576
15.980
1.00
45.62


ATOM
1527
CG
GLU
A
232
−6.968
48.493
16.558
1.00
54.23


ATOM
1528
CD
GLU
A
232
−7.022
49.891
15.976
1.00
63.62


ATOM
1529
OE1
GLU
A
232
−8.006
50.216
15.274
1.00
43.57


ATOM
1530
OE2
GLU
A
232
−6.079
50.564
16.211
1.00
59.06


ATOM
1531
N
ARG
A
233
−8.977
48.363
19.061
1.00
50.02


ATOM
1532
CA
ARG
A
233
−8.750
48.267
20.503
1.00
50.18


ATOM
1533
C
ARG
A
233
−10.035
47.647
21.221
1.00
54.57


ATOM
1534
O
ARG
A
233
−9.994
47.195
22.267
1.00
53.32


ATOM
1535
CB
ARG
A
233
−8.257
49.600
21.063
1.00
49.94


ATOM
1536
CG
ARG
A
233
−6.744
49.730
21.084
1.00
59.51


ATOM
1537
CD
ARG
A
233
−6.292
50.851
22.011
1.00
65.81


ATOM
1538
NE
ARG
A
233
−6.386
50.471
23.421
1.00
70.44


ATOM
1539
CZ
ARG
A
233
−6.209
51.316
24.434
1.00
81.89


ATOM
1540
NH1
ARG
A
233
−5.925
52.590
24.191
1.00
66.53


ATOM
1541
NH2
ARG
A
233
−6.308
50.886
25.689
1.00
67.48


ATOM
1542
N
LEU
A
234
−11.171
48.237
20.657
1.00
52.34


ATOM
1543
CA
LEU
A
234
−12.465
47.885
21.230
1.00
53.00


ATOM
1544
C
LEU
A
234
−12.836
46.436
20.863
1.00
59.29


ATOM
1545
O
LEU
A
234
−13.784
45.866
21.412
1.00
58.86


ATOM
1546
CB
LEU
A
234
−13.546
48.842
20.712
1.00
52.81


ATOM
1547
CG
LEU
A
234
−13.608
50.241
21.330
1.00
57.07


ATOM
1548
CD1
LEU
A
234
−14.767
51.036
20.735
1.00
57.03


ATOM
1549
CD2
LEU
A
234
−13.727
50.167
22.857
1.00
58.36


ATOM
1550
N
GLN
A
235
−12.084
45.857
19.924
1.00
57.12


ATOM
1551
CA
GLN
A
235
−12.339
44.504
19.444
1.00
57.49


ATOM
1552
C
GLN
A
235
−11.287
43.515
19.937
1.00
64.01


ATOM
1553
O
GLN
A
235
−11.041
42.493
19.299
1.00
63.07


ATOM
1554
CB
GLN
A
235
−12.372
44.488
17.916
1.00
58.66


ATOM
1555
CG
GLN
A
235
−13.761
44.520
17.306
1.00
72.25


ATOM
1556
CD
GLN
A
235
−13.766
44.060
15.853
1.00
95.60


ATOM
1557
OE1
GLN
A
235
−12.726
43.679
15.304
1.00
90.27


ATOM
1558
NE2
GLN
A
235
−14.936
44.099
15.222
1.00
91.08


ATOM
1559
N
GLY
A
236
−10.661
43.835
21.065
1.00
63.03


ATOM
1560
CA
GLY
A
236
−9.645
42.976
21.652
1.00
64.03


ATOM
1561
C
GLY
A
236
−8.364
42.928
20.821
1.00
72.04


ATOM
1562
O
GLY
A
236
−7.274
42.708
21.356
1.00
72.29


ATOM
1563
N
THR
A
237
−8.498
43.116
19.512
1.00
71.23


ATOM
1564
CA
THR
A
237
−7.341
43.089
18.609
1.00
72.15


ATOM
1565
C
THR
A
237
−6.237
44.019
19.107
1.00
79.00


ATOM
1566
O
THR
A
237
−6.447
45.231
19.223
1.00
79.19


ATOM
1567
CB
THR
A
237
−7.737
43.509
17.191
1.00
78.52


ATOM
1568
OG1
THR
A
237
−8.179
42.361
16.459
1.00
78.52


ATOM
1569
CG2
THR
A
237
−6.558
44.143
16.478
1.00
76.79


ATOM
1570
N
HIS
A
238
−5.063
43.455
19.398
1.00
76.83


ATOM
1571
CA
HIS
A
238
−3.950
44.256
19.907
1.00
77.21


ATOM
1572
C
HIS
A
238
−3.682
45.490
19.064
1.00
79.37


ATOM
1573
O
HIS
A
238
−3.833
45.474
17.839
1.00
79.17


ATOM
1574
CB
HIS
A
238
−2.668
43.419
20.134
1.00
78.73


ATOM
1575
CG
HIS
A
238
−2.000
43.693
21.451
1.00
82.79


ATOM
1576
ND1
HIS
A
238
−2.712
43.918
22.612
1.00
84.91


ATOM
1577
CD2
HIS
A
238
−0.692
43.815
21.783
1.00
85.02


ATOM
1578
CE1
HIS
A
238
−1.871
44.150
23.606
1.00
84.54


ATOM
1579
NE2
HIS
A
238
−0.639
44.094
23.129
1.00
84.88


ATOM
1580
N
TYR
A
239
−3.348
46.580
19.742
1.00
74.16


ATOM
1581
CA
TYR
A
239
−3.161
47.868
19.098
1.00
72.66


ATOM
1582
C
TYR
A
239
−1.723
48.361
19.113
1.00
71.95


ATOM
1583
O
TYR
A
239
−0.858
47.808
19.798
1.00
71.05


ATOM
1584
CB
TYR
A
239
−4.046
48.906
19.787
1.00
74.18


ATOM
1585
CG
TYR
A
239
−3.789
49.012
21.279
1.00
76.43


ATOM
1586
CD1
TYR
A
239
−3.962
47.909
22.118
1.00
78.45


ATOM
1587
CD2
TYR
A
239
−3.343
50.201
21.844
1.00
77.20


ATOM
1588
CE1
TYR
A
239
−3.713
47.997
23.479
1.00
79.20


ATOM
1589
CE2
TYR
A
239
−3.097
50.299
23.204
1.00
78.14


ATOM
1590
CZ
TYR
A
239
−3.283
49.194
24.017
1.00
84.83


ATOM
1591
OH
TYR
A
239
−3.038
49.294
25.369
1.00
84.64


ATOM
1592
N
SER
A
240
−1.494
49.442
18.381
1.00
65.44


ATOM
1593
CA
SER
A
240
−0.195
50.084
18.322
1.00
63.57


ATOM
1594
C
SER
A
240
−0.407
51.583
18.442
1.00
62.93


ATOM
1595
O
SER
A
240
−1.426
52.034
18.974
1.00
61.99


ATOM
1596
CB
SER
A
240
0.490
49.767
16.997
1.00
67.56


ATOM
1597
OG
SER
A
240
−0.428
49.860
15.921
1.00
78.32


ATOM
1598
N
VAL
A
241
0.544
52.355
17.925
1.00
56.50


ATOM
1599
CA
VAL
A
241
0.438
53.810
17.945
1.00
54.43


ATOM
1600
C
VAL
A
241
−0.729
54.202
17.064
1.00
53.69


ATOM
1601
O
VAL
A
241
−1.331
55.263
17.235
1.00
52.19


ATOM
1602
CB
VAL
A
241
1.723
54.480
17.412
1.00
58.22


ATOM
1603
CG1
VAL
A
241
2.153
53.840
16.100
1.00
58.15


ATOM
1604
CG2
VAL
A
241
1.521
55.982
17.244
1.00
57.96


ATOM
1605
N
GLN
A
242
−1.048
53.324
16.124
1.00
48.07


ATOM
1606
CA
GLN
A
242
−2.150
53.543
15.207
1.00
47.01


ATOM
1607
C
GLN
A
242
−3.430
53.835
15.969
1.00
49.12


ATOM
1608
O
GLN
A
242
−4.253
54.628
15.529
1.00
48.70


ATOM
1609
CB
GLN
A
242
−2.345
52.317
14.309
1.00
48.00


ATOM
1610
CG
GLN
A
242
−1.253
52.144
13.254
1.00
48.14


ATOM
1611
CD
GLN
A
242
−1.112
53.359
12.363
1.00
57.51


ATOM
1612
OE1
GLN
A
242
−0.223
54.188
12.557
1.00
51.74


ATOM
1613
NE2
GLN
A
242
−1.998
53.476
11.384
1.00
49.04


ATOM
1614
N
SER
A
243
−3.594
53.182
17.115
1.00
44.55


ATOM
1615
CA
SER
A
243
−4.789
53.364
17.931
1.00
43.48


ATOM
1616
C
SER
A
243
−4.918
54.794
18.455
1.00
44.15


ATOM
1617
O
SER
A
243
−6.028
55.311
18.615
1.00
43.93


ATOM
1618
CB
SER
A
243
−4.800
52.378
19.082
1.00
47.31


ATOM
1619
OG
SER
A
243
−5.982
51.610
19.059
1.00
58.55


ATOM
1620
N
ASP
A
244
−3.778
55.422
18.706
1.00
38.29


ATOM
1621
CA
ASP
A
244
−3.718
56.791
19.198
1.00
37.23


ATOM
1622
C
ASP
A
244
−4.109
57.789
18.088
1.00
40.90


ATOM
1623
O
ASP
A
244
−4.744
58.814
18.352
1.00
40.12


ATOM
1624
CB
ASP
A
244
−2.301
57.103
19.704
1.00
38.06


ATOM
1625
CG
ASP
A
244
−2.026
56.510
21.068
1.00
41.20


ATOM
1626
OD1
ASP
A
244
−2.995
56.234
21.816
1.00
39.57


ATOM
1627
OD2
ASP
A
244
−0.836
56.337
21.402
1.00
46.32


ATOM
1628
N
ILE
A
245
−3.741
57.462
16.851
1.00
37.01


ATOM
1629
CA
ILE
A
245
−4.066
58.297
15.694
1.00
36.60


ATOM
1630
C
ILE
A
245
−5.583
58.371
15.480
1.00
39.44


ATOM
1631
O
ILE
A
245
−6.122
59.420
15.102
1.00
39.33


ATOM
1632
CB
ILE
A
245
−3.373
57.774
14.422
1.00
39.90


ATOM
1633
CG1
ILE
A
245
−1.844
58.013
14.511
1.00
40.18


ATOM
1634
CG2
ILE
A
245
−3.990
58.397
13.165
1.00
39.98


ATOM
1635
CD1
ILE
A
245
−1.064
57.462
13.336
1.00
45.69


ATOM
1636
N
TRP
A
246
−6.276
57.276
15.770
1.00
34.70


ATOM
1637
CA
TRP
A
246
−7.723
57.250
15.642
1.00
34.03


ATOM
1638
C
TRP
A
246
−8.317
58.186
16.693
1.00
39.14


ATOM
1639
O
TRP
A
246
−9.202
58.994
16.403
1.00
39.66


ATOM
1640
CB
TRP
A
246
−8.267
55.823
15.838
1.00
32.42


ATOM
1641
CG
TRP
A
246
−9.727
55.804
16.235
1.00
33.11


ATOM
1642
CD1
TRP
A
246
−10.250
56.054
17.476
1.00
35.87


ATOM
1643
CD2
TRP
A
246
−10.847
55.592
15.366
1.00
32.86


ATOM
1644
NE1
TRP
A
246
−11.628
56.023
17.426
1.00
35.26


ATOM
1645
CE2
TRP
A
246
−12.015
55.728
16.144
1.00
36.61


ATOM
1646
CE3
TRP
A
246
−10.973
55.255
14.016
1.00
33.92


ATOM
1647
CZ2
TRP
A
246
−13.285
55.573
15.610
1.00
36.05


ATOM
1648
CZ3
TRP
A
246
−12.242
55.128
13.482
1.00
35.26


ATOM
1649
CH2
TRP
A
246
−13.379
55.284
14.279
1.00
35.99


ATOM
1650
N
SER
A
247
−7.839
58.052
17.926
1.00
35.34


ATOM
1651
CA
SER
A
247
−8.327
58.886
19.025
1.00
34.77


ATOM
1652
C
SER
A
247
−8.120
60.372
18.690
1.00
39.27


ATOM
1653
O
SER
A
247
−8.983
61.217
18.987
1.00
39.62


ATOM
1654
CB
SER
A
247
−7.605
58.519
20.332
1.00
36.72


ATOM
1655
OG
SER
A
247
−7.735
57.129
20.614
1.00
40.72


ATOM
1656
N
MET
A
248
−6.986
60.686
18.054
1.00
34.47


ATOM
1657
CA
MET
A
248
−6.700
62.056
17.676
1.00
33.71


ATOM
1658
C
MET
A
248
−7.695
62.533
16.647
1.00
37.49


ATOM
1659
O
MET
A
248
−8.298
63.601
16.800
1.00
36.81


ATOM
1660
CB
MET
A
248
−5.292
62.192
17.115
1.00
35.68


ATOM
1661
CG
MET
A
248
−5.021
63.580
16.556
1.00
38.44


ATOM
1662
SD
MET
A
248
−3.407
63.746
15.872
1.00
41.69


ATOM
1663
CE
MET
A
248
−2.642
62.909
14.284
1.00
38.33


ATOM
1664
N
GLY
A
249
−7.856
61.742
15.585
1.00
33.96


ATOM
1665
CA
GLY
A
249
−8.793
62.071
14.506
1.00
33.35


ATOM
1666
C
GLY
A
249
−10.205
62.275
15.044
1.00
37.26


ATOM
1667
O
GLY
A
249
−10.899
63.230
14.665
1.00
37.23


ATOM
1668
N
LEU
A
250
−10.625
61.387
15.938
1.00
33.37


ATOM
1669
CA
LEU
A
250
−11.961
61.474
16.530
1.00
33.22


ATOM
1670
C
LEU
A
250
−12.112
62.754
17.379
1.00
35.88


ATOM
1671
O
LEU
A
250
−13.137
63.432
17.320
1.00
34.13


ATOM
1672
CB
LEU
A
250
−12.278
60.215
17.368
1.00
33.29


ATOM
1673
CG
LEU
A
250
−13.663
60.232
18.033
1.00
38.11


ATOM
1674
CD1
LEU
A
250
−14.759
60.499
17.011
1.00
38.43


ATOM
1675
CD2
LEU
A
250
−13.948
58.975
18.824
1.00
39.75


ATOM
1676
N
SER
A
251
−11.077
63.066
18.161
1.00
32.69


ATOM
1677
CA
SER
A
251
−11.054
64.272
19.011
1.00
32.03


ATOM
1678
C
SER
A
251
−11.067
65.549
18.173
1.00
36.57


ATOM
1679
O
SER
A
251
−11.695
66.544
18.547
1.00
36.60


ATOM
1680
CB
SER
A
251
−9.802
64.283
19.890
1.00
33.33


ATOM
1681
OG
SER
A
251
−9.766
63.173
20.746
1.00
38.09


ATOM
1682
N
LEU
A
252
−10.328
65.532
17.068
1.00
33.15


ATOM
1683
CA
LEU
A
252
−10.246
66.691
16.188
1.00
32.96


ATOM
1684
C
LEU
A
252
−11.611
66.997
15.585
1.00
36.34


ATOM
1685
O
LEU
A
252
−11.984
68.153
15.425
1.00
35.46


ATOM
1686
CB
LEU
A
252
−9.238
66.438
15.058
1.00
32.80


ATOM
1687
CG
LEU
A
252
−7.767
66.612
15.396
1.00
36.90


ATOM
1688
CD1
LEU
A
252
−6.901
66.216
14.208
1.00
35.89


ATOM
1689
CD2
LEU
A
252
−7.482
68.062
15.839
1.00
39.05


ATOM
1690
N
VAL
A
253
−12.336
65.952
15.209
1.00
33.26


ATOM
1691
CA
VAL
A
253
−13.660
66.129
14.609
1.00
32.75


ATOM
1692
C
VAL
A
253
−14.622
66.685
15.635
1.00
36.73


ATOM
1693
O
VAL
A
253
−15.436
67.565
15.341
1.00
36.06


ATOM
1694
CB
VAL
A
253
−14.223
64.808
14.088
1.00
36.39


ATOM
1695
CG1
VAL
A
253
−15.711
64.956
13.747
1.00
36.02


ATOM
1696
CG2
VAL
A
253
−13.406
64.301
12.878
1.00
35.99


ATOM
1697
N
GLU
A
254
−14.543
66.169
16.851
1.00
34.39


ATOM
1698
CA
GLU
A
254
−15.432
66.647
17.900
1.00
34.59


ATOM
1699
C
GLU
A
254
−15.228
68.135
18.103
1.00
39.54


ATOM
1700
O
GLU
A
254
−16.154
68.890
18.230
1.00
40.30


ATOM
1701
CB
GLU
A
254
−15.175
65.923
19.209
1.00
35.77


ATOM
1702
CG
GLU
A
254
−15.770
66.652
20.414
1.00
42.66


ATOM
1703
CD
GLU
A
254
−15.763
65.812
21.672
1.00
46.98


ATOM
1704
OE1
GLU
A
254
−15.032
64.808
21.729
1.00
47.97


ATOM
1705
OE2
GLU
A
254
−16.480
66.162
22.609
1.00
38.11


ATOM
1706
N
MET
A
255
−13.961
68.552
18.142
1.00
34.84


ATOM
1707
CA
MET
A
255
−13.610
65.946
18.369
1.00
34.34


ATOM
1708
C
MET
A
255
−13.990
70.867
17.217
1.00
38.21


ATOM
1709
O
MET
A
255
−14.365
72.019
17.439
1.00
37.92


ATOM
1710
CB
MET
A
255
−12.123
70.081
18.724
1.00
36.58


ATOM
1711
CG
MET
A
255
−11.762
69.459
20.079
1.00
39.99


ATOM
1712
SD
MET
A
255
−10.009
69.532
20.479
1.00
44.63


ATOM
1713
CE
MET
A
255
−9.300
68.690
19.115
1.00
40.89


ATOM
1714
N
ALA
A
256
−13.920
70.355
15.993
1.00
34.69


ATOM
1715
CA
ALA
A
256
−14.271
71.147
14.809
1.00
35.09


ATOM
1716
C
ALA
A
256
−15.772
71.409
14.700
1.00
39.54


ATOM
1717
O
ALA
A
256
−16.193
72.473
14.264
1.00
39.51


ATOM
1718
CB
ALA
A
256
−13.769
70.464
13.536
1.00
35.81


ATOM
1719
N
VAL
A
257
−16.571
70.415
15.054
1.00
36.59


ATOM
1720
CA
VAL
A
257
−18.012
70.541
14.953
1.00
36.86


ATOM
1721
C
VAL
A
257
−18.693
70.955
16.264
1.00
41.56


ATOM
1722
O
VAL
A
257
−19.832
71.407
16.260
1.00
41.07


ATOM
1723
CB
VAL
A
257
−18.658
69.267
14.340
1.00
40.04


ATOM
1724
CG1
VAL
A
257
−17.971
68.930
13.022
1.00
39.35


ATOM
1725
CG2
VAL
A
257
−18.564
68.105
15.301
1.00
39.65


ATOM
1726
N
GLY
A
258
−17.971
70.839
17.373
1.00
40.71


ATOM
1727
CA
GLY
A
258
−18.487
71.277
18.675
1.00
41.19


ATOM
1728
C
GLY
A
258
−19.295
70.235
19.459
1.00
45.62


ATOM
1729
O
GLY
A
258
−19.987
70.573
20.419
1.00
46.28


ATOM
1730
N
ARG
A
259
−19.171
68.975
19.088
1.00
41.79


ATOM
1731
CA
ARG
A
259
−19.870
67.916
19.815
1.00
41.55


ATOM
1732
C
ARG
A
259
−19.272
66.526
19.525
1.00
42.91


ATOM
1733
O
ARG
A
259
−18.682
66.306
18.463
1.00
40.41


ATOM
1734
CB
ARG
A
259
−21.373
67.957
19.504
1.00
42.53


ATOM
1735
CG
ARG
A
259
−22.009
66.608
19.291
1.00
56.82


ATOM
1736
CD
ARG
A
259
−23.022
66.648
18.163
1.00
67.52


ATOM
1737
NE
ARG
A
259
−22.790
65.579
17.200
1.00
76.54


ATOM
1738
CZ
ARG
A
259
−23.582
64.524
17.041
1.00
88.17


ATOM
1739
NH1
ARG
A
259
−24.680
64.397
17.765
1.00
71.02


ATOM
1740
NH2
ARG
A
259
−23.273
63.599
16.151
1.00
79.09


ATOM
1741
N
TYR
A
260
−19.375
65.615
20.494
1.00
39.24


ATOM
1742
CA
TYR
A
260
−18.871
64.257
20.294
1.00
39.40


ATOM
1743
C
TYR
A
260
−19.555
63.725
19.036
1.00
45.95


ATOM
1744
O
TYR
A
260
−20.778
63.598
18.998
1.00
46.24


ATOM
1745
CB
TYR
A
260
−19.185
63.364
21.510
1.00
39.59


ATOM
1746
CG
TYR
A
260
−18.707
61.934
21.347
1.00
39.52


ATOM
1747
CD1
TYR
A
260
−17.363
61.607
21.508
1.00
41.05


ATOM
1748
CD2
TYR
A
260
−19.584
60.926
20.964
1.00
39.59


ATOM
1749
CE1
TYR
A
260
−16.916
60.308
21.324
1.00
40.63


ATOM
1750
CE2
TYR
A
260
−19.154
59.627
20.783
1.00
40.11


ATOM
1751
CZ
TYR
A
260
−17.818
59.321
20.997
1.00
45.42


ATOM
1752
OH
TYR
A
260
−17.388
58.027
20.820
1.00
43.61


ATOM
1753
N
PRO
A
261
−18.757
63.485
17.996
1.00
44.51


ATOM
1754
CA
PRO
A
261
−19.247
63.116
16.656
1.00
44.93


ATOM
1755
C
PRO
A
261
−20.110
61.860
16.426
1.00
51.80


ATOM
1756
O
PRO
A
261
−20.771
61.761
15.395
1.00
52.12


ATOM
1757
CB
PRO
A
261
−17.964
63.046
15.822
1.00
46.41


ATOM
1758
CG
PRO
A
261
−16.889
62.711
16.806
1.00
50.34


ATOM
1759
CD
PRO
A
261
−17.286
63.404
18.093
1.00
45.43


ATOM
1760
N
ILE
A
262
−20.070
60.890
17.335
1.00
49.56


ATOM
1761
CA
ILE
A
262
−20.855
59.659
17.153
1.00
50.17


ATOM
1762
C
ILE
A
262
−22.081
59.622
18.071
1.00
56.19


ATOM
1763
O
ILE
A
262
−21.970
59.870
19.263
1.00
55.52


ATOM
1764
CB
ILE
A
262
−20.007
58.394
17.418
1.00
53.16


ATOM
1765
CG1
ILE
A
262
−18.738
58.412
16.571
1.00
53.07


ATOM
1766
CG2
ILE
A
262
−20.821
57.142
17.145
1.00
53.96


ATOM
1767
CD1
ILE
A
262
−17.788
57.297
16.879
1.00
56.29


ATOM
1768
N
PRO
A
263
−23.245
59.304
17.509
1.00
54.73


ATOM
1769
CA
PRO
A
263
−23.378
59.001
16.092
1.00
54.90


ATOM
1770
C
PRO
A
263
−23.434
60.301
15.306
1.00
60.28


ATOM
1771
O
PRO
A
263
−23.647
61.359
15.874
1.00
59.26


ATOM
1772
CB
PRO
A
263
−24.739
58.324
16.031
1.00
56.24


ATOM
1773
CG
PRO
A
263
−25.557
59.056
17.110
1.00
60.45


ATOM
1774
CD
PRO
A
263
−24.543
59.675
18.095
1.00
55.55


ATOM
1775
N
PRO
A
264
−23.266
60.210
13.994
1.00
59.41


ATOM
1776
CA
PRO
A
264
−23.252
61.397
13.141
1.00
60.04


ATOM
1777
C
PRO
A
264
−24.461
62.316
13.304
1.00
67.53


ATOM
1778
O
PRO
A
264
−25.574
61.870
13.596
1.00
66.22


ATOM
1779
CB
PRO
A
264
−23.190
60.815
11.718
1.00
61.12


ATOM
1780
CG
PRO
A
264
−23.625
59.408
11.855
1.00
65.08


ATOM
1781
CD
PRO
A
264
−23.197
58.968
13.211
1.00
60.10


ATOM
1782
N
PRO
A
265
−24.222
63.611
13.120
1.00
67.91


ATOM
1783
CA
PRO
A
265
−25.277
64.612
13.218
1.00
68.88


ATOM
1784
C
PRO
A
265
−26.138
64.533
11.975
1.00
77.04


ATOM
1785
O
PRO
A
265
−25.623
64.415
10.861
1.00
76.47


ATOM
1786
CB
PRO
A
265
−24.504
65.937
13.217
1.00
70.10


ATOM
1787
CG
PRO
A
265
−23.166
65.594
13.765
1.00
74.07


ATOM
1788
CD
PRO
A
265
−22.879
64.188
13.318
1.00
68.89


ATOM
1789
N
ASP
A
266
−27.447
64.587
12.160
1.00
76.99


ATOM
1790
CA
ASP
A
266
−28.355
64.544
11.029
1.00
78.32


ATOM
1791
C
ASP
A
266
−28.347
65.905
10.324
1.00
84.64


ATOM
1792
O
ASP
A
266
−27.886
66.898
10.889
1.00
84.46


ATOM
1793
CB
ASP
A
266
−29.757
64.140
11.479
1.00
80.44


ATOM
1794
CG
ASP
A
266
−29.801
62.724
12.044
1.00
92.97


ATOM
1795
OD1
ASP
A
266
−29.069
61.849
11.525
1.00
93.71


ATOM
1796
OD2
ASP
A
266
−30.558
62.491
13.010
1.00
100.34


ATOM
1797
N
ALA
A
267
−28.790
65.924
9.069
1.00
82.74


ATOM
1798
CA
ALA
A
267
−28.777
67.143
8.249
1.00
83.30


ATOM
1799
C
ALA
A
267
−29.216
68.422
8.970
1.00
88.43


ATOM
1800
O
ALA
A
267
−28.535
69.448
8.895
1.00
88.02


ATOM
1801
CB
ALA
A
267
−29.577
66.941
6.972
1.00
84.08


ATOM
1802
N
LYS
A
268
−30.353
68.364
9.655
1.00
85.63


ATOM
1803
CA
LYS
A
268
−30.853
69.527
10.374
1.00
85.77


ATOM
1804
C
LYS
A
268
−29.885
69.929
11.478
1.00
90.02


ATOM
1805
O
LYS
A
268
−29.667
71.117
11.723
1.00
89.86


ATOM
1806
CB
LYS
A
268
−32.240
69.250
10.950
1.00
88.73


ATOM
1807
CG
LYS
A
268
−33.372
69.402
9.938
1.00
105.23


ATOM
1808
CD
LYS
A
268
−34.450
70.346
10.451
1.00
117.00


ATOM
1809
CE
LYS
A
268
−35.398
70.765
9.334
1.00
129.01


ATOM
1810
NZ
LYS
A
268
−34.853
71.903
8.536
1.00
137.93


ATOM
1811
N
GLU
A
269
−29.288
68.933
12.130
1.00
86.40


ATOM
1812
CA
GLU
A
269
−28.318
69.185
13.194
1.00
86.11


ATOM
1813
C
GLU
A
269
−27.173
70.059
12.678
1.00
89.14


ATOM
1814
O
GLU
A
269
−26.721
70.976
13.364
1.00
88.53


ATOM
1815
CB
GLU
A
269
−27.759
67.867
13.738
1.00
87.58


ATOM
1816
CG
GLU
A
269
−28.804
66.784
13.966
1.00
99.38


ATOM
1817
CD
GLU
A
269
−28.349
65.739
14.972
1.00
120.91


ATOM
1818
OE1
GLU
A
269
−27.879
66.129
16.063
1.00
112.93


ATOM
1819
OE2
GLU
A
269
−28.452
64.532
14.668
1.00
116.34


ATOM
1820
N
LEU
A
270
−26.710
69.759
11.465
1.00
85.10


ATOM
1821
CA
LEU
A
270
−25.623
70.508
10.839
1.00
84.75


ATOM
1822
C
LEU
A
270
−26.091
71.880
10.377
1.00
88.46


ATOM
1823
O
LEU
A
270
−25.323
72.844
10.374
1.00
87.87


ATOM
1824
CB
LEU
A
270
−25.070
69.735
9.644
1.00
84.71


ATOM
1825
CG
LEU
A
270
−24.150
68.563
9.966
1.00
89.32


ATOM
1826
CD1
LEU
A
270
−24.154
67.568
8.821
1.00
89.47


ATOM
1827
CD2
LEU
A
270
−22.739
69.056
10.255
1.00
91.41


ATOM
1828
N
GLU
A
271
−27.349
71.954
9.964
1.00
85.14


ATOM
1829
CA
GLU
A
271
−27.925
73.201
9.489
1.00
85.04


ATOM
1830
C
GLU
A
271
−27.949
74.241
10.608
1.00
88.48


ATOM
1831
O
GLU
A
271
−27.831
75.440
10.357
1.00
88.16


ATOM
1832
CB
GLU
A
271
−29.332
72.950
8.940
1.00
86.48


ATOM
1833
CG
GLU
A
271
−30.103
74.222
8.607
1.00
98.36


ATOM
1834
CD
GLU
A
271
−31.597
74.060
8.821
1.00
121.66


ATOM
1835
OE1
GLU
A
271
−32.222
73.259
8.090
1.00
117.24


ATOM
1836
OE2
GLU
A
271
−32.141
74.716
9.735
1.00
116.18


ATOM
1837
N
LEU
A
272
−28.079
73.774
11.845
1.00
84.60


ATOM
1838
CA
LEU
A
272
−28.096
74.669
12.998
1.00
84.29


ATOM
1839
C
LEU
A
272
−26.682
74.875
13.534
1.00
87.39


ATOM
1840
O
LEU
A
272
−26.407
75.846
14.245
1.00
86.84


ATOM
1841
CB
LEU
A
272
−28.995
74.107
14.106
1.00
84.43


ATOM
1842
CG
LEU
A
272
−30.312
73.446
13.689
1.00
89.31


ATOM
1843
CD1
LEU
A
272
−30.620
72.249
14.592
1.00
89.51


ATOM
1844
CD2
LEU
A
272
−31.458
74.457
13.714
1.00
91.38


ATOM
1845
N
MET
A
273
−25.789
73.946
13.198
1.00
83.23


ATOM
1846
CA
MET
A
273
−24.407
74.003
13.661
1.00
82.55


ATOM
1847
C
MET
A
273
−23.565
74.978
12.853
1.00
86.09


ATOM
1848
O
MET
A
273
−22.795
75.755
13.413
1.00
85.80


ATOM
1849
CB
MET
A
273
−23.771
72.612
13.626
1.00
84.70


ATOM
1850
CG
MET
A
273
−24.332
71.651
14.656
1.00
88.11


ATOM
1851
SD
MET
A
273
−23.820
69.956
14.359
1.00
92.11


ATOM
1852
CE
MET
A
273
−22.237
69.934
15.194
1.00
88.81


ATOM
1853
N
PHE
A
274
−23.703
74.923
11.535
1.00
82.38


ATOM
1854
CA
PHE
A
274
−22.932
75.788
10.660
1.00
82.08


ATOM
1855
C
PHE
A
274
−23.820
76.581
9.708
1.00
86.39


ATOM
1856
O
PHE
A
274
−23.360
77.523
9.057
1.00
85.67


ATOM
1857
CB
PHE
A
274
−21.906
74.969
9.875
1.00
83.65


ATOM
1858
CG
PHE
A
274
−20.970
74.172
10.743
1.00
84.93


ATOM
1859
CD1
PHE
A
274
−21.350
72.939
11.246
1.00
87.88


ATOM
1860
CD2
PHE
A
274
−19.704
74.650
11.045
1.00
86.85


ATOM
1861
CE1
PHE
A
274
−20.487
72.200
12.033
1.00
88.61


ATOM
1862
CE2
PHE
A
274
−18.840
73.916
11.836
1.00
89.50


ATOM
1863
CZ
PHE
A
274
−19.231
72.692
12.328
1.00
87.57


ATOM
1864
N
GLY
A
275
−25.093
76.196
9.631
1.00
83.49


ATOM
1865
CA
GLY
A
275
−26.047
76.873
8.756
1.00
83.22


ATOM
1866
C
GLY
A
275
−25.831
76.487
7.293
1.00
86.68


ATOM
1867
O
GLY
A
275
−26.099
77.275
6.391
1.00
86.36


ATOM
1868
N
CYS
A
276
−25.226
75.323
7.078
1.00
82.69


ATOM
1869
N
PRO
A
305
−31.367
57.249
21.703
1.00
79.39


ATOM
1870
CA
PRO
A
305
−30.844
58.581
22.018
1.00
78.71


ATOM
1871
C
PRO
A
305
−31.442
59.131
23.320
1.00
81.45


ATOM
1872
O
PRO
A
305
−32.665
59.208
23.468
1.00
81.69


ATOM
1873
CB
PRO
A
305
−31.302
59.424
20.823
1.00
80.36


ATOM
1874
CG
PRO
A
305
−32.545
58.754
20.347
1.00
84.73


ATOM
1875
CD
PRO
A
305
−32.359
57.280
20.610
1.00
80.02


ATOM
1876
N
PRO
A
306
−30.574
59.509
24.259
1.00
76.27


ATOM
1877
CA
PRO
A
306
−29.134
59.415
24.056
1.00
74.96


ATOM
1878
C
PRO
A
306
−28.666
57.966
23.977
1.00
75.88


ATOM
1879
O
PRO
A
306
−29.331
57.052
24.479
1.00
75.99


ATOM
1880
CB
PRO
A
306
−28.567
60.088
25.304
1.00
76.76


ATOM
1881
CG
PRO
A
306
−29.592
61.105
25.665
1.00
81.46


ATOM
1882
CD
PRO
A
306
−30.922
60.483
25.312
1.00
76.79


ATOM
1883
N
MET
A
307
−27.527
57.762
23.326
1.00
69.14


ATOM
1884
CA
MET
A
307
−26.964
56.434
23.167
1.00
67.41


ATOM
1885
C
MET
A
307
−26.166
56.028
24.404
1.00
67.82


ATOM
1886
O
MET
A
307
−25.322
56.790
24.895
1.00
66.61


ATOM
1887
CB
MET
A
307
−26.060
56.397
21.931
1.00
69.63


ATOM
1888
CG
MET
A
307
−26.009
55.052
21.214
1.00
73.12


ATOM
1889
SD
MET
A
307
−24.996
55.120
19.704
1.00
77.00


ATOM
1890
CE
MET
A
307
−25.888
54.023
18.633
1.00
73.84


ATOM
1891
N
ALA
A
308
−26.434
54.824
24.906
1.00
62.03


ATOM
1892
CA
ALA
A
308
−25.693
54.300
26.042
1.00
60.52


ATOM
1893
C
ALA
A
308
−24.283
53.964
25.568
1.00
61.86


ATOM
1894
O
ALA
A
308
−24.058
53.718
24.379
1.00
60.70


ATOM
1895
CB
ALA
A
308
−26.380
53.058
26.608
1.00
61.15


ATOM
1896
N
ILE
A
309
−23.332
53.991
26.494
1.00
57.37


ATOM
1897
CA
ILE
A
309
−21.936
53.710
26.176
1.00
56.39


ATOM
1898
C
ILE
A
309
−21.780
52.427
25.362
1.00
56.76


ATOM
1899
O
ILE
A
309
−21.111
52.421
24.322
1.00
56.28


ATOM
1900
CB
ILE
A
309
−21.072
53.614
27.457
1.00
59.77


ATOM
1901
CG1
ILE
A
309
−21.602
54.579
28.523
1.00
60.91


ATOM
1902
CG2
ILE
A
309
−19.614
53.898
27.145
1.00
59.83


ATOM
1903
CD1
ILE
A
309
−20.506
55.261
29.360
1.00
71.52


ATOM
1904
N
PHE
A
310
−22.401
51.344
25.830
1.00
50.33


ATOM
1905
CA
PHE
A
310
−22.300
50.057
25.146
1.00
48.82


ATOM
1906
C
PHE
A
310
−22.818
50.104
23.711
1.00
52.35


ATOM
1907
O
PHE
A
310
−22.236
49.495
22.813
1.00
51.80


ATOM
1903
CB
PHE
A
310
−22.956
48.922
25.958
1.00
49.98


ATOM
1909
CG
PHE
A
310
−24.306
49.273
26.532
1.00
51.02


ATOM
1910
CD1
PHE
A
310
−25.465
49.069
25.793
1.00
54.02


ATOM
1911
CD2
PHE
A
310
−24.420
49.758
27.827
1.00
52.75


ATOM
1912
CE1
PHE
A
310
−26.713
49.371
26.327
1.00
55.15


ATOM
1913
CE2
PHE
A
310
−25.662
50.070
28.369
1.00
55.52


ATOM
1914
CZ
PHE
A
310
−26.810
49.876
27.621
1.00
53.88


ATOM
1915
N
GLU
A
311
−23.901
50.849
23.496
1.00
49.46


ATOM
1916
CA
GLU
A
311
−24.465
51.020
22.154
1.00
49.23


ATOM
1917
C
GLU
A
311
−23.479
51.825
21.325
1.00
52.61


ATOM
1918
O
GLU
A
311
−23.239
51.536
20.153
1.00
53.06


ATOM
1919
CB
GLU
A
311
−25.796
51.759
22.227
1.00
50.52


ATOM
1920
CG
GLU
A
311
−26.791
51.138
23.177
1.00
61.40


ATOM
1921
CD
GLU
A
311
−27.998
52.020
23.416
1.00
78.78


ATOM
1922
OE1
GLU
A
311
−27.811
53.223
23.679
1.00
76.19


ATOM
1923
OE2
GLU
A
311
−29.133
51.510
23.325
1.00
70.35


ATOM
1924
N
LEU
A
312
−22.881
52.817
21.965
1.00
48.00


ATOM
1925
CA
LEU
A
312
−21.879
53.651
21.337
1.00
47.83


ATOM
1926
C
LEU
A
312
−20.686
52.805
20.893
1.00
50.63


ATOM
1927
O
LEU
A
312
−20.279
52.845
19.731
1.00
49.42


ATOM
1928
CB
LEU
A
312
−21.403
54.716
22.332
1.00
48.12


ATOM
1929
CG
LEU
A
312
−20.867
56.026
21.772
1.00
52.84


ATOM
1930
CD1
LEU
A
312
−20.198
56.817
22.876
1.00
52.64


ATOM
1931
CD2
LEU
A
312
−19.906
55.767
20.625
1.00
55.74


ATOM
1932
N
LEU
A
313
−20.114
52.056
21.831
1.00
47.36


ATOM
1933
CA
LEU
A
313
−18.956
51.223
21.525
1.00
47.10


ATOM
1934
C
LEU
A
313
−19.221
50.281
20.351
1.00
52.03


ATOM
1935
O
LEU
A
313
−18.396
50.161
19.445
1.00
51.92


ATOM
1936
CB
LEU
A
313
−18.481
50.465
22.761
1.00
46.82


ATOM
1937
CG
LEU
A
313
−17.979
51.352
23.909
1.00
51.06


ATOM
1938
CD1
LEU
A
313
−17.103
50.560
24.864
1.00
50.80


ATOM
1939
CD2
LEU
A
313
−17.228
52.584
23.370
1.00
52.11


ATOM
1940
N
ASP
A
314
−20.398
49.668
20.334
1.00
49.39


ATOM
1941
CA
ASP
A
314
−20.767
48.768
19.240
1.00
49.73


ATOM
1942
C
ASP
A
314
−20.843
49.536
17.922
1.00
53.72


ATOM
1943
O
ASP
A
314
−20.319
49.088
16.898
1.00
53.43


ATOM
1944
CB
ASP
A
314
−22.104
48.079
19.537
1.00
52.04


ATOM
1945
CG
ASP
A
314
−22.525
47.137
18.437
1.00
65.24


ATOM
1946
OD1
ASP
A
314
−21.938
46.038
18.334
1.00
66.13


ATOM
1947
OD2
ASP
A
314
−23.435
47.500
17.664
1.00
73.57


ATOM
1948
N
TYR
A
315
−21.471
50.710
17.964
1.00
49.98


ATOM
1949
CA
TYR
A
315
−21.577
51.575
16.794
1.00
49.89


ATOM
1950
C
TYR
A
315
−20.192
51.859
16.205
1.00
52.91


ATOM
1951
O
TYR
A
315
−19.958
51.648
15.020
1.00
53.30


ATOM
1952
CB
TYR
A
315
−22.267
52.891
17.173
1.00
51.89


ATOM
1953
CG
TYR
A
315
−22.639
53.764
15.988
1.00
54.75


ATOM
1954
CD1
TYR
A
315
−21.660
54.416
15.239
1.00
56.67


ATOM
1955
CD2
TYR
A
315
−23.975
53.947
15.627
1.00
55.99


ATOM
1956
CE1
TYR
A
315
−21.998
55.213
14.154
1.00
57.96


ATOM
1957
CE2
TYR
A
315
−24.327
54.748
14.545
1.00
57.16


ATOM
1958
CZ
TYR
A
315
−23.339
55.377
13.812
1.00
66.34


ATOM
1959
OH
TYR
A
315
−23.692
56.166
12.741
1.00
68.75


ATOM
1960
N
ILE
A
316
−19.274
52.329
17.045
1.00
48.17


ATOM
1961
CA
ILE
A
316
−17.912
52.625
16.612
1.00
47.32


ATOM
1962
C
ILE
A
316
−17.304
51.423
15.897
1.00
51.41


ATOM
1963
O
ILE
A
316
−16.662
51.562
14.860
1.00
51.04


ATOM
1964
CB
ILE
A
316
−16.999
52.993
17.818
1.00
50.14


ATOM
1965
CG1
ILE
A
316
−17.464
54.303
18.476
1.00
50.42


ATOM
1966
CG2
ILE
A
316
−15.522
53.073
17.389
1.00
50.06


ATOM
1967
CD1
ILE
A
316
−16.778
54.606
19.804
1.00
51.78


ATOM
1968
N
VAL
A
317
−17.501
50.240
16.466
1.00
48.13


ATOM
1969
CA
VAL
A
317
−16.938
49.021
15.899
1.00
47.88


ATOM
1970
C
VAL
A
317
−17.647
48.555
14.631
1.00
51.42


ATOM
1971
O
VAL
A
317
−17.015
48.011
13.724
1.00
50.45


ATOM
1972
CB
VAL
A
317
−16.967
47.865
16.915
1.00
51.65


ATOM
1973
CG1
VAL
A
317
−16.600
46.542
16.233
1.00
51.16


ATOM
1974
CG2
VAL
A
317
−16.040
48.158
18.080
1.00
51.40


ATOM
1975
N
ASN
A
318
−18.958
48.748
14.575
1.00
48.32


ATOM
1976
CA
ASN
A
318
−19.733
48.260
13.441
1.00
48.50


ATOM
1977
C
ASN
A
318
−20.117
49.259
12.358
1.00
52.96


ATOM
1978
O
ASN
A
318
−20.445
48.864
11.247
1.00
53.20


ATOM
1979
CB
ASN
A
318
−20.952
47.486
13.921
1.00
48.15


ATOM
1980
CG
ASN
A
318
−20.574
46.262
14.717
1.00
63.75


ATOM
1981
OD1
ASN
A
318
−19.811
45.410
14.245
1.00
58.36


ATOM
1982
ND2
ASN
A
318
−21.042
46.197
15.955
1.00
52.36


ATOM
1983
N
GLU
A
319
−20.091
50.547
12.678
1.00
49.15


ATOM
1984
CA
GLU
A
319
−20.451
51.569
11.701
1.00
48.57


ATOM
1985
C
GLU
A
319
−19.235
52.134
10.983
1.00
51.92


ATOM
1986
O
GLU
A
319
−18.096
51.794
11.295
1.00
52.07


ATOM
1987
CB
GLU
A
319
−21.220
52.707
12.377
1.00
49.86


ATOM
1988
CG
GLU
A
319
−22.688
52.405
12.632
1.00
58.62


ATOM
1989
CD
GLU
A
319
−23.281
51.486
11.583
1.00
79.38


ATOM
1990
OE1
GLU
A
319
−23.588
51.967
10.472
1.00
74.71


ATOM
1991
OE2
GLU
A
319
−23.432
50.283
11.866
1.00
74.57


ATOM
1992
N
PRO
A
320
−19.486
53.011
10.019
1.00
47.91


ATOM
1993
CA
PRO
A
320
−18.408
53.684
9.299
1.00
46.72


ATOM
1994
C
PRO
A
320
−17.963
54.876
10.139
1.00
47.84


ATOM
1995
O
PRO
A
320
−18.782
55.508
10.823
1.00
46.64


ATOM
1996
CB
PRO
A
320
−19.092
54.153
8.014
1.00
48.52


ATOM
1997
CG
PRO
A
320
−20.151
53.118
7.775
1.00
53.08


ATOM
1998
CD
PRO
A
320
−20.654
52.748
9.153
1.00
48.47


ATOM
1999
N
PRO
A
321
−16.663
55.142
10.144
1.00
43.00


ATOM
2000
CA
PRO
A
321
−16.121
56.215
10.966
1.00
42.19


ATOM
2001
C
PRO
A
321
−16.752
57.561
10.624
1.00
46.31


ATOM
2002
O
PRO
A
321
−17.115
57.819
9.472
1.00
45.59


ATOM
2003
CB
PRO
A
321
−14.633
56.209
10.614
1.00
43.62


ATOM
2004
CG
PRO
A
321
−14.575
55.673
9.213
1.00
47.50


ATOM
2005
CD
PRO
A
321
−15.742
54.742
9.058
1.00
42.74


ATOM
2006
N
PRO
A
322
−16.895
58.410
11.635
1.00
42.82


ATOM
2007
CA
PRO
A
322
−17.452
59.743
11.434
1.00
42.57


ATOM
2008
C
PRO
A
322
−16.575
60.548
10.472
1.00
45.65


ATOM
2009
O
PRO
A
322
−15.494
60.101
10.054
1.00
44.99


ATOM
2010
CB
PRO
A
322
−17.386
60.374
12.840
1.00
44.21


ATOM
2011
CG
PRO
A
322
−16.698
59.319
13.745
1.00
48.02


ATOM
2012
CD
PRO
A
322
−16.049
58.345
12.834
1.00
43.10


ATOM
2013
N
LYS
A
323
−17.023
61.743
10.148
1.00
41.27


ATOM
2014
CA
LYS
A
323
−16.272
62.596
9.268
1.00
40.96


ATOM
2015
C
LYS
A
323
−16.749
64.025
9.381
1.00
44.57


ATOM
2016
O
LYS
A
323
−17.859
64.292
9.842
1.00
44.58


ATOM
2017
CB
LYS
A
323
−16.393
62.108
7.819
1.00
43.88


ATOM
2018
CG
LYS
A
323
−17.724
62.442
7.161
1.00
55.19


ATOM
2019
CD
LYS
A
323
−17.944
61.597
5.921
1.00
63.53


ATOM
2020
CE
LYS
A
323
−19.424
61.348
5.686
1.00
70.60


ATOM
2021
NZ
LYS
A
323
−20.012
62.356
4.766
1.00
79.07


ATOM
2022
N
LEU
A
324
−15.918
64.950
8.937
1.00
40.44


ATOM
2023
CA
LEU
A
324
−16.279
66.349
8.981
1.00
39.81


ATOM
2024
C
LEU
A
324
−17.348
66.625
7.956
1.00
45.49


ATOM
2025
O
LEU
A
324
−17.355
66.030
6.878
1.00
45.04


ATOM
2026
CB
LEU
A
324
−15.069
67.215
8.675
1.00
39.28


ATOM
2027
CG
LEU
A
324
−13.998
67.263
9.750
1.00
42.51


ATOM
2028
CD1
LEU
A
324
−12.708
67.818
9.161
1.00
41.94


ATOM
2029
CD2
LEU
A
324
−14.485
68.111
10.927
1.00
43.16


ATOM
2030
N
PRO
A
325
−18.231
67.561
8.270
1.00
43.11


ATOM
2031
CA
PRO
A
325
−19.257
67.968
7.320
1.00
43.00


ATOM
2032
C
PRO
A
325
−18.534
68.667
6.181
1.00
47.42


ATOM
2033
O
PRO
A
325
−17.523
69.343
6.400
1.00
46.56


ATOM
2034
CB
PRO
A
325
−20.086
68.988
8.115
1.00
44.66


ATOM
2035
CG
PRO
A
325
−19.156
69.482
9.174
1.00
48.51


ATOM
2036
CD
PRO
A
325
−18.339
68.290
9.543
1.00
43.48


ATOM
2037
N
SER
A
326
−19.031
68.487
4.967
1.00
45.11


ATOM
2038
CA
SER
A
326
−18.399
69.082
3.801
1.00
45.46


ATOM
2039
C
SER
A
326
−18.854
70.509
3.551
1.00
49.85


ATOM
2040
O
SER
A
326
−19.930
70.914
3.982
1.00
49.34


ATOM
2041
CB
SER
A
326
−18.629
68.216
2.561
1.00
49.79


ATOM
2042
OG
SER
A
326
−19.998
68.199
2.212
1.00
60.68


ATOM
2043
N
GLY
A
327
−18.020
71.269
2.862
1.00
47.39


ATOM
2044
CA
GLY
A
327
−18.337
72.657
2.545
1.00
47.28


ATOM
2045
C
GLY
A
327
−17.757
73.631
3.572
1.00
51.46


ATOM
2046
O
GLY
A
327
−17.237
74.691
3.212
1.00
51.98


ATOM
2047
N
VAL
A
328
−17.842
73.271
4.848
1.00
46.47


ATOM
2048
CA
VAL
A
328
−17.356
74.150
5.913
1.00
45.15


ATOM
2049
C
VAL
A
328
−15.871
74.022
6.253
1.00
45.14


ATOM
2050
O
VAL
A
328
−15.306
74.897
6.887
1.00
45.13


ATOM
2051
CB
VAL
A
328
−18.211
74.039
7.186
1.00
49.31


ATOM
2052
CG1
VAL
A
328
−19.491
74.817
7.012
1.00
49.29


ATOM
2053
CG2
VAL
A
328
−18.508
72.582
7.510
1.00
49.12


ATOM
2054
N
PHE
A
329
−15.248
72.928
5.842
1.00
38.62


ATOM
2055
CA
PHE
A
329
−13.830
72.723
6.121
1.00
36.85


ATOM
2056
C
PHE
A
329
−13.070
72.468
4.845
1.00
38.65


ATOM
2057
O
PHE
A
329
−13.640
72.015
3.861
1.00
38.79


ATOM
2058
CB
PHE
A
329
−13.634
71.553
7.088
1.00
38.07


ATOM
2059
CG
PHE
A
329
−14.283
71.762
8.420
1.00
38.83


ATOM
2060
CD1
PHE
A
329
−13.674
72.555
9.387
1.00
40.53


ATOM
2061
CD2
PHE
A
329
−15.511
71.192
8.702
1.00
40.39


ATOM
2062
CE1
PHE
A
329
−14.269
72.761
10.604
1.00
40.80


ATOM
2063
CE2
PHE
A
329
−16.105
71.382
9.935
1.00
42.80


ATOM
2064
CZ
PHE
A
329
−15.484
72.182
10.882
1.00
40.52


ATOM
2065
N
SER
A
330
−11.776
72.761
4.857
1.00
33.45


ATOM
2066
CA
SER
A
330
−10.960
72.542
3.675
1.00
33.02


ATOM
2067
C
SEF
A
330
−10.895
71.047
3.357
1.00
37.70


ATOM
2068
O
SER
A
330
−11.059
70.210
4.231
1.00
37.53


ATOM
2069
CB
SER
A
330
−9.548
73.114
3.862
1.00
34.22


ATOM
2070
OG
SER
A
330
−8.805
72.324
4.773
1.00
38.23


ATOM
+2071
N
LEU
A
331
−10.657
70.727
2.099
1.00
34.97


ATOM
2072
CA
LEU
A
331
−10.560
69.344
1.674
1.00
34.84


ATOM
2073
C
LEU
A
331
−9.353
68.724
2.320
1.00
38.81


ATOM
2074
O
LEU
A
331
−9.375
67.552
2.703
1.00
40.25


ATOM
2075
CB
LEU
A
331
−10.454
69.270
0.152
1.00
35.16


ATOM
2076
CG
LEU
A
331
−11.787
69.396
−0.597
1.00
40.25


ATOM
2077
CD1
LEU
A
331
−11.562
69.401
−2.093
1.00
40.72


ATOM
2078
CD2
LEU
A
331
−12.706
68.250
−0.198
1.00
43.38


ATOM
2079
N
GLU
A
332
−8.305
69.521
2.494
1.00
33.28


ATOM
2080
CA
GLU
A
332
−7.092
69.034
3.142
1.00
32.14


ATOM
2081
C
GLU
A
332
−7.344
68.602
4.581
1.00
35.58


ATOM
2082
O
GLU
A
332
−6.825
67.567
5.020
1.00
36.88


ATOM
2083
CB
GLU
A
332
−5.979
70.062
3.054
1.00
33.18


ATOM
2084
CG
GLU
A
332
−5.519
70.299
1.622
1.00
42.68


ATOM
2085
CD
GLU
A
332
−4.486
71.382
1.516
1.00
57.24


ATOM
2086
OE1
GLU
A
332
−4.536
72.331
2.318
1.00
48.84


ATOM
2087
OE2
GLU
A
332
−3.609
71.277
0.638
1.00
53.58


ATOM
2088
N
PHE
A
333
−8.169
69.368
5.302
1.00
29.27


ATOM
2089
CA
PHE
A
333
−8.524
69.026
6.684
1.00
28.28


ATOM
2090
C
PHE
A
333
−9.396
67.760
6.708
1.00
33.22


ATOM
2091
O
PHE
A
333
−9.085
66.800
7.422
1.00
32.97


ATOM
2092
CB
PHE
A
333
−9.239
70.198
7.383
1.00
29.50


ATOM
2093
CG
PHE
A
333
−9.413
70.006
8.864
1.00
30.19


ATOM
2094
CD1
PHE
A
333
−8.549
69.171
9.583
1.00
31.83


ATOM
2095
CD2
PHE
A
333
−10.462
70.628
9.546
1.00
30.96


ATOM
2096
CE1
PHE
A
333
−8.696
69.010
10.960
1.00
31.39


ATOM
2097
CE2
PHE
A
333
−10.615
70.455
10.904
1.00
32.99


ATOM
2098
CZ
PHE
A
333
−9.722
69.646
11.612
1.00
30.97


ATOM
2099
N
GLN
A
334
−10.464
67.747
5.908
1.00
30.24


ATOM
2100
CA
GLN
A
334
−11.324
66.558
5.796
1.00
30.66


ATOM
2101
C
GLN
A
334
−10.501
65.291
5.432
1.00
36.69


ATOM
2102
O
GLN
A
334
−10.717
64.214
5.994
1.00
37.96


ATOM
2103
CB
GLN
A
334
−12.416
65.766
4.730
1.00
31.63


ATOM
2104
CG
GLN
A
334
−13.291
67.977
4.945
1.00
33.35


ATOM
2105
CD
GLN
A
334
−14.273
68.185
3.808
1.00
41.34


ATOM
2106
OE1
GLN
A
334
−14.979
67.270
3.412
1.00
35.55


ATOM
2107
NE2
GLN
A
334
−14.292
69.383
3.259
1.00
30.24


ATOM
2108
N
ASP
A
335
−9.582
65.418
4.482
1.00
32.37


ATOM
2109
CA
ASP
A
335
−8.772
64.269
4.089
1.00
32.22


ATOM
2110
C
ASP
A
335
−7.893
63.821
5.259
1.00
37.26


ATOM
2111
O
ASP
A
335
−7.756
62.621
5.524
1.00
38.52


ATOM
2112
CB
ASP
A
335
−7.924
64.573
2.839
1.00
33.42


ATOM
2113
CG
ASP
A
335
−7.064
63.365
2.392
1.00
37.13


ATOM
2114
OD1
ASP
A
335
−7.633
62.400
1.829
1.00
36.78


ATOM
2115
OD2
ASP
A
335
−5.818
63.417
2.558
1.00
37.00


ATOM
2116
N
PHE
A
336
−7.321
64.788
5.971
1.00
32.39


ATOM
2117
CA
PHE
A
336
−6.466
64.489
7.124
1.00
31.25


ATOM
2118
C
PHE
A
336
−7.212
63.660
8.179
1.00
36.05


ATOM
2119
O
PHE
A
336
−6.716
62.626
8.628
1.00
36.42


ATOM
2120
CB
PHE
A
336
−5.916
65.782
7.744
1.00
32.10


ATOM
2121
CG
PHE
A
336
−5.075
65.559
8.972
1.00
32.43


ATOM
2122
CD1
PHE
A
336
−3.710
65.321
8.863
1.00
34.34


ATOM
2123
CD2
PHE
A
336
−5.651
65.573
10.237
1.00
33.54


ATOM
2124
CE1
PHE
A
336
−2.930
65.107
10.004
1.00
34.94


ATOM
2125
CE2
PHE
A
336
−4.884
65.355
11.372
1.00
36.13


ATOM
2126
CZ
PHE
A
336
−3.519
65.139
11.258
1.00
34.28


ATOM
2127
N
VAL
A
337
−8.402
64.114
8.572
1.00
32.46


ATOM
2128
CA
VAL
A
337
−9.206
63.383
9.559
1.00
32.33


ATOM
2129
C
VAL
A
337
−9.614
62.024
8.999
1.00
37.81


ATOM
2130
O
VAL
A
337
−9.502
61.014
9.679
1.00
37.74


ATOM
2131
CB
VAL
A
337
−10.485
64.166
9.990
1.00
35.40


ATOM
2132
CG1
VAL
A
337
−10.114
65.442
10.762
1.00
34.97


ATOM
2133
CG2
VAL
A
337
−11.329
64.488
8.798
1.00
35.00


ATOM
2134
N
ASN
A
338
−10.075
62.008
7.746
1.00
34.89


ATOM
2135
CA
ASN
A
338
−10.455
60.762
7.087
1.00
34.59


ATOM
2136
C
ASN
A
338
−9.311
59.740
7.170
1.00
39.26


ATOM
2137
O
ASN
A
338
−9.530
58.556
7.459
1.00
39.04


ATOM
2138
CB
ASN
A
338
−10.774
61.073
5.614
1.00
32.62


ATOM
2139
CG
ASN
A
338
−12.187
61.534
5.394
1.00
42.83


ATOM
2140
OD1
ASN
A
338
−12.912
61.813
6.331
1.00
38.77


ATOM
2141
ND2
ASN
A
338
−12.560
61.685
4.142
1.00
32.76


ATOM
2142
N
LYS
A
339
−8.092
60.189
6.898
1.00
35.70


ATOM
2143
CA
LYS
A
339
−6.940
59.282
6.919
1.00
35.70


ATOM
2144
C
LYS
A
339
−6.605
58.794
8.334
1.00
41.19


ATOM
2145
O
LYS
A
339
−5.907
57.781
8.508
1.00
41.35


ATOM
2146
CB
LYS
A
339
−5.729
59.927
6.241
1.00
37.26


ATOM
2147
CG
LYS
A
339
−5.736
59.822
4.694
1.00
36.84


ATOM
2148
CD
LYS
A
339
−4.334
60.076
4.110
1.00
41.70


ATOM
2149
CE
LYS
A
339
−4.387
60.323
2.598
1.00
40.95


ATOM
2150
NZ
LYS
A
339
−5.688
59.883
2.046
1.00
46.62


ATOM
2151
N
CYS
A
340
−7.091
59.529
9.336
1.00
37.53


ATOM
2152
CA
CYS
A
340
−6.875
59.194
10.746
1.00
37.14


ATOM
2153
C
CYS
A
340
−7.966
58.231
11.240
1.00
40.99


ATOM
2154
O
CYS
A
340
−7.751
57.463
12.177
1.00
39.72


ATOM
2155
CB
CYS
A
340
−6.954
60.477
11.603
1.00
37.33


ATOM
2156
SG
CYS
A
340
−5.449
61.483
11.706
1.00
41.16


ATOM
2157
N
LEU
A
341
−9.160
58.340
10.654
1.00
38.00


ATOM
2158
CA
LEU
A
341
−10.307
57.565
11.114
1.00
38.15


ATOM
2159
C
LEU
A
341
−10.628
56.306
10.300
1.00
44.15


ATOM
2160
O
LEU
A
341
−11.738
55.760
10.383
1.00
43.60


ATOM
2161
CB
LEU
A
341
−11.529
58.465
11.256
1.00
37.90


ATOM
2162
CG
LEU
A
341
−11.329
59.537
12.335
1.00
42.02


ATOM
2163
CD1
LEU
A
341
−12.565
60.391
12.532
1.00
41.53


ATOM
2164
CD2
LEU
A
341
−10.899
58.892
13.639
1.00
44.03


ATOM
2165
N
ILE
A
342
−9.645
55.841
9.535
1.00
41.76


ATOM
2166
CA
ILE
A
342
−9.782
54.623
8.761
1.00
41.83


ATOM
2167
C
ILE
A
342
−9.766
53.444
9.749
1.00
47.02


ATOM
2168
O
ILE
A
342
−8.823
53.300
10.541
1.00
46.00


ATOM
2169
CB
ILE
A
342
−8.622
54.470
7.768
1.00
44.80


ATOM
2170
CG1
ILE
A
342
−8.855
55.348
6.528
1.00
44.35


ATOM
2171
CG2
ILE
A
342
−8.429
52.995
7.390
1.00
46.30


ATOM
2172
CD1
ILE
A
342
−7.597
55.665
5.750
1.00
39.39


ATOM
2173
N
LYS
A
343
−10.835
52.646
9.735
1.00
44.65


ATOM
2174
CA
LYS
A
343
−10.974
51.507
10.656
1.00
45.01


ATOM
2175
C
LYS
A
343
−9.836
50.459
10.605
1.00
49.70


ATOM
2176
O
LYS
A
343
−9.447
49.915
11.626
1.00
49.07


ATOM
2177
CB
LYS
A
343
−12.343
50.852
10.504
1.00
47.44


ATOM
2178
CG
LYS
A
343
−13.434
51.821
10.054
1.00
60.81


ATOM
2179
CD
LYS
A
343
−14.594
51.847
11.028
1.00
67.81


ATOM
2180
CE
LYS
A
343
−15.575
50.727
10.743
1.00
69.65


ATOM
2181
NZ
LYS
A
343
−16.390
50.391
11.935
1.00
68.48


ATOM
2182
N
ASN
A
344
−9.296
50.202
9.425
1.00
47.38


ATOM
2183
CA
ASN
A
344
−8.194
49.256
9.309
1.00
47.80


ATOM
2184
C
ASN
A
344
−6.899
49.948
9.712
1.00
51.62


ATOM
2185
O
ASN
A
344
−6.337
50.735
8.946
1.00
51.01


ATOM
2186
CB
ASN
A
344
−8.093
48.710
7.874
1.00
50.39


ATOM
2187
CG
ASN
A
344
−6.964
47.687
7.700
1.00
70.04


ATOM
2188
OD1
ASN
A
344
−6.069
47.570
8.540
1.00
59.25


ATOM
2189
ND2
ASN
A
344
−6.988
46.975
6.582
1.00
64.14


ATOM
2190
N
PRO
A
345
−6.431
49.651
10.918
1.00
48.57


ATOM
2191
CA
PRO
A
345
−5.209
50.262
11.436
1.00
48.01


ATOM
2192
C
PRO
A
345
−4.064
50.122
10.447
1.00
52.08


ATOM
2193
O
PRO
A
345
−3.113
50.913
10.458
1.00
51.83


ATOM
2194
CB
PRO
A
345
−4.920
49.458
12.720
1.00
49.24


ATOM
2195
CG
PRO
A
345
−5.713
48.225
12.604
1.00
53.44


ATOM
2196
CD
PRO
A
345
−6.917
48.568
11.784
1.00
49.02


ATOM
2197
N
ALA
A
346
−4.167
49.121
9.577
1.00
48.25


ATOM
2198
CA
ALA
A
346
−3.136
48.877
8.570
1.00
47.92


ATOM
2199
C
ALA
A
346
−3.191
49.949
7.484
1.00
50.25


ATOM
2200
O
ALA
A
346
−2.164
50.477
7.058
1.00
49.06


ATOM
2201
CB
ALA
A
346
−3.309
47.482
7.962
1.00
48.79


ATOM
2202
N
GLU
A
347
−4.404
50.261
7.044
1.00
46.91


ATOM
2203
CA
GLU
A
347
−4.613
51.277
6.029
1.00
46.99


ATOM
2204
C
GLU
A
347
−4.417
52.664
6.643
1.00
49.74


ATOM
2205
O
GLU
A
347
−3.809
53.545
6.029
1.00
48.84


ATOM
2206
CB
GLU
A
347
−6.028
51.169
5.463
1.00
46.77


ATOM
2207
CG
GLU
A
347
−6.295
49.905
4.678
1.00
63.75


ATOM
2208
CD
GLU
A
347
−7.701
49.870
4.113
1.00
96.20


ATOM
2209
OE1
GLU
A
347
−8.615
49.393
4.821
1.00
97.37


ATOM
2210
OE2
GLU
A
347
−7.900
50.360
2.977
1.00
96.17


ATOM
2211
N
ARG
A
348
−4.963
52.839
7.854
1.00
44.97


ATOM
2212
CA
ARG
A
348
−4.897
54.089
8.597
1.00
43.31


ATOM
2213
C
ARG
A
348
−3.515
54.707
8.526
1.00
46.50


ATOM
2214
O
ARG
A
348
−2.514
54.002
8.555
1.00
46.48


ATOM
2215
CB
ARG
A
348
−5.301
53.857
10.054
1.00
41.29


ATOM
2216
CG
ARG
A
348
−5.542
55.139
10.850
1.00
44.45


ATOM
2217
CD
ARG
A
348
−6.040
54.843
12.264
1.00
43.28


ATOM
2218
NE
ARG
A
348
−7.104
53.837
12.282
1.00
43.15


ATOM
2219
CZ
ARG
A
348
−7.283
52.959
13.268
1.00
50.47


ATOM
2220
NH1
ARG
A
348
−6.466
52.953
14.315
1.00
39.02


ATOM
2221
NH2
ARG
A
348
−8.270
52.086
13.208
1.00
35.19


ATOM
2222
N
ALA
A
349
−3.467
56.025
8.381
1.00
42.62


ATOM
2223
CA
ALA
A
349
−2.199
56.732
8.268
1.00
42.22


ATOM
2224
C
ALA
A
349
−1.372
56.599
9.526
1.00
46.23


ATOM
2225
O
ALA
A
349
−1.907
56.402
10.611
1.00
46.28


ATOM
2226
CB
ALA
A
349
−2.438
58.188
7.947
1.00
43.07


ATOM
2227
N
ASP
A
350
−0.057
56.721
9.383
1.00
42.78


ATOM
2228
CA
ASP
A
350
0.838
56.618
10.526
1.00
42.33


ATOM
2229
C
ASP
A
350
1.542
57.935
10.843
1.00
44.38


ATOM
2230
O
ASP
A
350
1.488
58.883
10.058
1.00
43.34


ATOM
2231
CB
ASP
A
350
1.832
55.443
10.367
1.00
44.34


ATOM
2232
CG
ASP
A
350
2.874
55.683
9.275
1.00
57.12


ATOM
2233
OD1
ASP
A
350
2.956
56.808
8.737
1.00
57.71


ATOM
2234
OD2
ASP
A
350
3.631
54.737
8.969
1.00
64.19


ATOM
2235
N
LEU
A
351
2.181
57.992
12.002
1.00
40.61


ATOM
2236
CA
LEU
A
351
2.840
59.209
12.454
1.00
40.60


ATOM
2237
C
LEU
A
351
3.716
59.863
11.404
1.00
45.29


ATOM
2238
O
LEU
A
351
3.714
61.085
11.255
1.00
45.97


ATOM
2239
CB
LEU
A
351
3.638
58.957
13.736
1.00
40.33


ATOM
2240
CG
LEU
A
351
2.829
58.740
15.017
1.00
44.15


ATOM
2241
CD1
LEU
A
351
3.748
58.528
16.189
1.00
44.21


ATOM
2242
CD2
LEU
A
351
1.870
59.887
15.272
1.00
45.14


ATOM
2243
N
LYS
A
352
4.469
59.052
10.679
1.00
41.88


ATOM
2244
CA
LYS
A
352
5.390
59.561
9.666
1.00
41.48


ATOM
2245
C
LYS
A
352
4.651
60.185
8.500
1.00
43.92


ATOM
2246
O
LYS
A
352
5.034
61.229
8.001
1.00
43.42


ATOM
2247
CB
LYS
A
352
6.316
58.438
9.175
1.00
44.12


ATOM
2248
CG
LYS
A
352
7.121
58.787
7.933
1.00
62.12


ATOM
2249
CD
LYS
A
352
8.523
58.191
7.999
1.00
73.09


ATOM
2250
CE
LYS
A
352
9.210
58.216
6.643
1.00
80.18


ATOM
2251
NZ
LYS
A
352
10.604
58.735
6.742
1.00
87.82


ATOM
2252
N
GLN
A
353
3.580
59.539
8.077
1.00
40.36


ATOM
2253
CA
GLN
A
353
2.792
60.021
6.956
1.00
39.75


ATOM
2254
C
GLN
A
353
2.054
61.287
7.328
1.00
45.00


ATOM
2255
O
GLN
A
353
2.006
62.235
6.558
1.00
45.89


ATOM
2256
CB
GLN
A
353
1.799
58.952
6.509
1.00
40.51


ATOM
2257
CG
GLN
A
353
2.445
57.657
6.045
1.00
48.12


ATOM
2258
CD
GLN
A
353
1.422
56.559
5.774
1.00
65.18


ATOM
2259
OE1
GLN
A
353
0.256
56.670
6.155
1.00
60.77


ATOM
2260
NE2
GLN
A
353
1.852
55.509
5.100
1.00
55.21


ATOM
2261
N
LEU
A
354
1.467
61.296
8.520
1.00
40.66


ATOM
2262
CA
LEU
A
354
0.736
62.459
8.984
1.00
39.79


ATOM
2263
C
LEU
A
354
1.610
63.699
9.041
1.00
43.41


ATOM
2264
O
LEU
A
354
1.194
64.766
8.610
1.00
42.46


ATOM
2265
CB
LEU
A
354
0.074
62.181
10.326
1.00
39.82


ATOM
2266
CG
LEU
A
354
−1.012
61.106
10.237
1.00
44.45


ATOM
2267
CD1
LEU
A
354
−1.499
60.686
11.608
1.00
44.83


ATOM
2268
CD2
LEU
A
354
−2.163
61.563
9.359
1.00
45.68


ATOM
2269
N
MET
A
355
2.840
63.550
9.521
1.00
40.74


ATOM
2270
CA
MET
A
355
3.760
64.684
9.610
1.00
41.52


ATOM
2271
C
MET
A
355
3.945
65.406
8.275
1.00
44.68


ATOM
2272
O
MET
A
355
4.226
66.616
8.243
1.00
43.59


ATOM
2273
CB
MET
A
355
5.114
64.245
10.167
1.00
44.89


ATOM
2274
CG
MET
A
355
5.265
64.450
11.682
1.00
50.02


ATOM
2275
SD
MET
A
355
5.168
66.209
12.171
1.00
55.56


ATOM
2276
CE
MET
A
355
3.433
66.361
12.511
1.00
52.58


ATOM
2277
N
VAL
A
356
3.801
64.664
7.172
1.00
40.68


ATOM
2278
CA
VAL
A
356
3.948
65.239
5.847
1.00
39.65


ATOM
2279
C
VAL
A
356
2.629
65.356
5.070
1.00
41.64


ATOM
2280
O
VAL
A
356
2.621
65.708
3.883
1.00
41.57


ATOM
2281
CB
VAL
A
356
5.030
64.524
5.024
1.00
43.95


ATOM
2282
CG1
VAL
A
356
6.380
64.626
5.746
1.00
44.15


ATOM
2283
CG2
VAL
A
356
4.653
63.055
4.780
1.00
43.54


ATOM
2284
N
HIS
A
357
1.513
65.108
5.752
1.00
35.73


ATOM
2285
CA
HIS
A
357
0.204
65.258
5.124
1.00
34.05


ATOM
2286
C
HIS
A
357
0.009
66.733
4.761
1.00
37.68


ATOM
2287
O
HIS
A
357
0.482
67.626
5.480
1.00
37.19


ATOM
2288
CB
HIS
A
357
−0.906
64.792
6.073
1.00
34.03


ATOM
2289
CG
HIS
A
357
−2.267
64.771
5.444
1.00
36.92


ATOM
2290
ND1
HIS
A
357
−3.003
65.918
5.219
1.00
38.26


ATOM
2291
CD2
HIS
A
357
−3.019
63.744
4.980
1.00
37.92


ATOM
2292
CE1
HIS
A
357
−4.157
65.593
4.664
1.00
37.28


ATOM
2293
NE2
HIS
A
357
−4.189
64.282
4.502
1.00
37.55


ATOM
2294
N
ALA
A
358
−0.640
66.978
3.620
1.00
33.50


ATOM
2295
CA
ALA
A
358
−0.868
68.335
3.107
1.00
32.56


ATOM
2296
C
ALA
A
358
−1.489
69.290
4.122
1.00
36.64


ATOM
2297
O
ALA
A
358
−1.272
70.512
4.057
1.00
37.11


ATOM
2298
CB
ALA
A
358
−1.710
68.288
1.876
1.00
33.16


ATOM
2299
N
PHE
A
359
−2.299
68.757
5.035
1.00
31.31


ATOM
2300
CA
PHE
A
359
−2.938
69.604
6.026
1.00
30.79


ATOM
2301
C
PHE
A
359
−1.945
70.049
7.075
1.00
36.81


ATOM
2302
O
PHE
A
359
−1.988
71.188
7.546
1.00
35.68


ATOM
2303
CB
PHE
A
359
−4.118
68.888
6.664
1.00
32.00


ATOM
2304
CG
PHE
A
359
−4.677
69.587
7.874
1.00
33.12


ATOM
2305
CD1
PHE
A
359
−5.380
70.765
7.743
1.00
35.48


ATOM
2306
CD2
PHE
A
359
−4.526
69.065
9.123
1.00
34.43


ATOM
2307
CE1
PHE
A
359
−5.875
71.443
8.849
1.00
35.90


ATOM
2308
CE2
PHE
A
359
−5.113
69.679
10.234
1.00
36.83


ATOM
2309
CZ
PHE
A
359
−5.802
70.861
10.078
1.00
34.97


ATOM
2310
N
ILE
A
360
−1.055
69.139
7.452
1.00
34.44


ATOM
2311
CA
ILE
A
360
−0.044
69.431
8.444
1.00
34.33


ATOM
2312
C
ILE
A
360
1.000
70.405
7.891
1.00
39.99


ATOM
2313
O
ILE
A
360
1.329
71.404
8.528
1.00
40.13


ATOM
2314
CB
ILE
A
360
0.629
68.130
8.946
1.00
36.87


ATOM
2315
CG1
ILE
A
360
−0.348
67.339
9.835
1.00
36.07


ATOM
2316
CG2
ILE
A
360
1.918
68.446
9.704
1.00
37.09


ATOM
2317
CD1
ILE
A
360
−1.053
68.203
10.909
1.00
31.13


ATOM
2318
N
LYS
A
361
1.478
70.134
6.686
1.00
37.87


ATOM
2319
CA
LYS
A
361
2.462
70.994
6.034
1.00
38.04


ATOM
2320
C
LYS
A
361
1.919
72.406
5.860
1.00
42.35


ATOM
2321
O
LYS
A
361
2.621
73.381
6.102
1.00
42.56


ATOM
2322
CB
LYS
A
361
2.865
70.412
4.679
1.00
40.74


ATOM
2323
CG
LYS
A
361
4.069
69.509
4.738
1.00
54.10


ATOM
2324
CD
LYS
A
361
3.829
68.225
3.976
1.00
65.94


ATOM
2325
CB
LYS
A
361
3.832
68.452
2.473
1.00
73.16


ATOM
2326
NZ
LYS
A
361
3.044
67.406
1.761
1.00
80.60


ATOM
2327
N
ARG
A
362
0.664
72.508
5.442
1.00
38.96


ATOM
2328
CA
ARG
A
362
0.016
73.809
5.280
1.00
38.95


ATOM
2329
C
ARG
A
362
−0.096
74.515
6.641
1.00
45.56


ATOM
2330
O
ARG
A
362
0.200
75.702
6.765
1.00
46.13


ATOM
2331
CB
ARG
A
362
−1.376
73.643
4.670
1.00
36.35


ATOM
2332
CG
ARG
A
362
−2.032
74.951
4.229
1.00
39.05


ATOM
2333
CD
ARG
A
362
−3.544
74.799
4.049
1.00
37.27


ATOM
2334
NE
ARG
A
362
−4.261
74.789
5.334
1.00
35.14


ATOM
2335
CZ
ARG
A
362
−5.460
74.244
5.518
1.00
41.42


ATOM
2336
NH1
ARG
A
362
−6.078
73.638
4.508
1.00
24.66


ATOM
2337
NH2
ARG
A
362
−6.046
74.303
6.708
1.00
25.38


ATOM
2338
N
SER
A
363
−0.496
73.761
7.659
1.00
42.40


ATOM
2339
CA
SER
A
363
−0.666
74.301
8.999
1.00
42.43


ATOM
2340
C
SER
A
363
0.646
74.818
9.575
1.00
48.61


ATOM
2341
O
SER
A
363
0.588
75.881
10.193
1.00
48.04


ATOM
2342
CB
SER
A
363
−1.270
73.246
9.930
1.00
44.67


ATOM
2343
OG
SER
A
363
−2.610
72.953
9.577
1.00
49.02


ATOM
2344
N
ASP
A
364
1.712
74.050
9.385
1.00
47.04


ATOM
2345
CA
ASP
A
364
3.027
74.422
9.898
1.00
47.11


ATOM
2346
C
ASP
A
364
3.492
75.765
9.350
1.00
50.65


ATOM
2347
O
ASP
A
364
4.144
76.539
10.053
1.00
50.84


ATOM
2348
CB
ASP
A
364
4.054
73.336
9.565
1.00
49.13


ATOM
2349
CG
ASP
A
364
4.897
72.930
10.774
1.00
61.15


ATOM
2350
OD1
ASP
A
364
5.157
73.793
11.639
1.00
62.63


ATOM
2351
OD2
ASP
A
364
5.326
71.753
10.840
1.00
66.63


ATOM
2352
N
ALA
A
365
3.161
76.036
8.092
1.00
46.50


ATOM
2353
CA
ALA
A
365
3.575
77.277
7.438
1.00
46.30


ATOM
2354
C
ALA
A
365
2.594
78.417
7.694
1.00
51.12


ATOM
2355
O
ALA
A
365
2.728
79.511
7.128
1.00
51.56


ATOM
2356
CB
ALA
A
365
3.753
77.054
5.934
1.00
46.87


ATOM
2357
N
GLU
A
366
1.590
78.151
8.516
1.00
46.89


ATOM
2358
CA
GLU
A
366
0.600
79.159
8.840
1.00
46.38


ATOM
2359
C
GLU
A
366
1.023
79.932
10.077
1.00
51.46


ATOM
2360
O
GLU
A
366
1.396
79.348
11.089
1.00
51.01


ATOM
2361
CB
GLU
A
366
−0.762
78.517
9.069
1.00
47.31


ATOM
2362
CG
GLU
A
366
−1.678
78.544
7.858
1.00
50.12


ATOM
2363
CD
GLU
A
366
−2.811
77.552
7.976
1.00
55.67


ATOM
2364
OE1
GLU
A
366
−3.017
77.013
9.090
1.00
37.31


ATOM
2365
OE2
GLU
A
366
−3.481
77.291
6.954
1.00
45.47


ATOM
2366
N
GLU
A
367
0.977
81.253
9.983
1.00
49.32


ATOM
2367
CA
GLU
A
367
1.329
82.114
11.111
1.00
49.62


ATOM
2368
C
GLU
A
367
0.076
82.330
11.906
1.00
52.60


ATOM
2369
O
GLU
A
367
−0.635
83.311
11.704
1.00
51.88


ATOM
2370
CB
GLU
A
367
1.878
83.470
10.623
1.00
51.35


ATOM
2371
CG
GLU
A
367
2.906
83.374
9.481
1.00
63.53


ATOM
2372
CD
GLU
A
367
4.099
82.509
9.839
1.00
88.72


ATOM
2373
OE1
GLU
A
367
4.104
81.916
10.939
1.00
83.80


ATOM
2374
OE2
GLU
A
367
5.043
82.414
9.016
1.00
87.05


ATOM
2375
N
VAL
A
368
−0.239
81.370
12.762
1.00
48.90


ATOM
2376
CA
VAL
A
368
−1.463
81.418
13.544
1.00
48.10


ATOM
2377
C
VAL
A
368
−1.156
81.731
14.999
1.00
49.60


ATOM
2378
O
VAL
A
368
−0.335
81.068
15.627
1.00
49.00


ATOM
2379
CB
VAL
A
368
−2.238
80.071
13.436
1.00
52.01


ATOM
2380
CG1
VAL
A
368
−3.298
79.964
14.509
1.00
51.80


ATOM
2381
CG2
VAL
A
368
−2.848
79.927
12.064
1.00
51.85


ATOM
2382
N
ASP
A
369
−1.795
82.766
15.527
1.00
44.47


ATOM
2383
CA
ASP
A
369
−1.574
83.150
16.913
1.00
43.03


ATOM
2384
C
ASP
A
369
−2.507
82.364
17.828
1.00
43.31


ATOM
2385
O
ASP
A
369
−3.615
82.798
18.131
1.00
44.11


ATOM
2386
CB
ASP
A
369
−1.772
84.648
17.105
1.00
44.59


ATOM
2387
CG
ASP
A
369
−1.469
85.088
18.508
1.00
54.79


ATOM
2388
OD1
ASP
A
369
−0.436
84.653
19.051
1.00
55.39


ATOM
2389
OD2
ASP
A
369
−2.291
85.820
19.091
1.00
63.47


ATOM
2390
N
PHE
A
370
−2.060
81.190
18.235
1.00
36.16


ATOM
2391
CA
PHE
A
370
−2.854
80.324
19.086
1.00
34.38


ATOM
2392
C
PHE
A
370
−3.081
80.938
20.473
1.00
37.05


ATOM
2393
O
PHE
A
370
−4.202
80.941
20.983
1.00
36.56


ATOM
2394
CB
PHE
A
370
−2.204
78.943
19.206
1.00
35.28


ATOM
2395
CG
PHE
A
370
−2.849
78.065
20.241
1.00
36.42


ATOM
2396
CD1
PHE
A
370
−4.107
77.542
20.031
1.00
39.84


ATOM
2397
CD2
PHE
A
370
−2.226
77.821
21.445
1.00
37.64


ATOM
2398
CE1
PHE
A
370
−4.716
76.757
20.995
1.00
40.63


ATOM
2399
CE2
PHE
A
370
−2.825
77.037
22.399
1.00
40.55


ATOM
2400
CZ
PHE
A
370
−4.066
76.504
22.175
1.00
38.96


ATOM
2401
N
ALA
A
371
−2.011
81.451
21.077
1.00
33.13


ATOM
2402
CA
ALA
A
371
−2.108
82.073
22.397
1.00
32.86


ATOM
2403
C
ALA
A
371
−3.178
83.145
22.401
1.00
36.60


ATOM
2404
O
ALA
A
371
−4.119
83.094
23.189
1.00
37.76


ATOM
2405
CB
ALA
A
371
−0.763
82.654
22.822
1.00
33.45


ATOM
2406
N
GLY
A
372
−3.037
84.112
21.507
1.00
32.47


ATOM
2407
CA
GLY
A
372
−4.006
85.194
21.392
1.00
32.13


ATOM
2408
C
GLY
A
372
−5.409
84.632
21.246
1.00
36.18


ATOM
2409
O
GLY
A
372
−6.297
84.978
22.014
1.00
36.34


ATOM
2410
N
TRP
A
373
−5.601
83.742
20.269
1.00
31.93


ATOM
2411
CA
TRP
A
373
−6.916
83.130
20.056
1.00
31.44


ATOM
2412
C
TRP
A
373
−7.391
82.472
21.323
1.00
36.35


ATOM
2413
O
TRP
A
373
−8.549
82.627
21.718
1.00
36.63


ATOM
2414
CB
TRP
A
373
−6.879
82.077
18.932
1.00
29.43


ATOM
2415
CG
TRP
A
373
−8.168
81.261
18.862
1.00
29.63


ATOM
2416
CD1
TRP
A
373
−9.273
81.533
18.101
1.00
32.47


ATOM
2417
CD2
TRP
A
373
−8.499
80.100
19.644
1.00
28.88


ATOM
2418
NE1
TRP
A
373
−10.258
80.604
18.347
1.00
31.57


ATOM
2419
CE2
TRP
A
373
−9.807
79.717
19.291
1.00
32.79


ATOM
2420
CE3
TRP
A
373
−7.810
79.339
20.590
1.00
29.57


ATOM
2421
CZ2
TRP
A
373
−10.436
78.605
19.851
1.00
32.00


ATOM
2422
CZ3
TRP
A
373
−8.437
78.242
21.145
1.00
30.75


ATOM
2423
CH2
TRP
A
373
−9.735
77.889
20.779
1.00
31.50


ATOM
2424
N
LEU
A
374
−6.500
81.717
21.960
1.00
33.16


ATOM
2425
CA
LEU
A
374
−6.856
81.017
23.192
1.00
33.50


ATOM
2426
C
LEU
A
374
−7.272
81.979
24.307
1.00
38.34


ATOM
2427
O
LEU
A
374
−8.301
81.788
24.945
1.00
37.68


ATOM
2428
CB
LEU
A
374
−5.717
80.111
23.662
1.00
33.58


ATOM
2429
CG
LEU
A
374
−5.899
79.531
25.076
1.00
38.67


ATOM
2430
CD1
LEU
A
374
−7.081
78.605
25.116
1.00
39.03


ATOM
2431
CD2
LEU
A
374
−4.646
78.819
25.547
1.00
40.78


ATOM
2432
N
CYS
A
375
−6.479
83.018
24.532
1.00
36.70


ATOM
2433
CA
CYS
A
375
−6.783
83.969
25.605
1.00
37.68


ATOM
2434
C
CYS
A
375
−8.110
84.704
25.449
1.00
39.93


ATOM
2435
O
CYS
A
375
−8.850
84.853
26.414
1.00
38.93


ATOM
2436
CB
CYS
A
375
−5.617
84.923
25.861
1.00
38.67


ATOM
2437
SG
CYS
A
375
−4.129
84.047
26.457
1.00
43.09


ATOM
2438
N
SER
A
376
−8.443
85.094
24.228
1.00
36.31


ATOM
2439
CA
SER
A
376
−9.722
85.776
23.981
1.00
36.59


ATOM
2440
C
SER
A
376
−10.911
84.828
24.086
1.00
39.80


ATOM
2441
O
SER
A
376
−11.995
85.223
24.495
1.00
39.05


ATOM
2442
CB
SER
A
376
−9.726
86.463
22.617
1.00
39.67


ATOM
2443
OG
SER
A
376
−8.459
86.384
22.023
1.00
51.54


ATOM
2444
N
THR
A
377
−10.695
83.575
23.722
1.00
36.28


ATOM
2445
CA
THR
A
377
−11.755
82.587
23.747
1.00
35.99


ATOM
2446
C
THR
A
377
−12.171
82.164
25.151
1.00
40.71


ATOM
2447
O
THR
A
377
−13.353
81.896
25.403
1.00
40.63


ATOM
2448
CB
THR
A
377
−11.384
81.355
22.927
1.00
40.94


ATOM
2449
OG1
THR
A
377
−11.143
81.751
21.575
1.00
36.69


ATOM
2450
CG2
THR
A
377
−12.503
80.339
22.965
1.00
38.93


ATOM
2451
N
ILE
A
378
−11.210
82.061
26.061
1.00
37.53


ATOM
2452
CA
ILE
A
378
−11.547
81.657
27.420
1.00
37.78


ATOM
2453
C
ILE
A
378
−11.534
82.800
28.409
1.00
43.45


ATOM
2454
O
ILE
A
378
−11.781
82.604
29.583
1.00
43.32


ATOM
2455
CB
ILE
A
378
−10.699
80.459
27.936
1.00
40.42


ATOM
2456
CG1
ILE
A
378
−9.272
80.883
28.245
1.00
40.30


ATOM
2457
CG2
ILE
A
378
−10.734
79.306
26.949
1.00
41.11


ATOM
2458
CD1
ILE
A
378
−8.379
79.720
28.602
1.00
45.64


ATOM
2459
N
GLY
A
379
−11.290
84.004
27.919
1.00
42.13


ATOM
2460
CA
GLY
A
379
−11.292
85.177
28.776
1.00
43.39


ATOM
2461
C
GLY
A
379
−10.072
85.173
29.674
1.00
51.72


ATOM
2462
O
GLY
A
379
−10.061
85.798
30.726
1.00
51.01


ATOM
2463
N
LEU
A
380
−9.035
84.476
29.238
1.00
52.39


ATOM
2464
CA
LEU
A
380
−7.813
84.392
30.000
1.00
54.24


ATOM
2465
C
LEU
A
380
−7.175
85.752
30.130
1.00
65.03


ATOM
2466
O
LEU
A
380
−6.759
86.354
29.139
1.00
64.33


ATOM
2467
CB
LEU
A
380
−6.838
83.434
29.337
1.00
54.22


ATOM
2468
CG
LEU
A
380
−6.458
82.212
30.161
1.00
58.89


ATOM
2469
CD1
LEU
A
380
−5.407
81.381
29.439
1.00
58.67


ATOM
2470
CD2
LEU
A
380
−5.956
82.652
31.520
1.00
61.91


ATOM
2471
N
ASN
A
381
−7.117
86.244
31.356
1.00
65.42


ATOM
2472
CA
ASN
A
381
−6.466
87.501
31.622
1.00
66.91


ATOM
2473
C
ASN
A
381
−5.059
87.160
32.081
1.00
75.34


ATOM
2474
O
ASN
A
381
−4.799
86.982
33.280
1.00
73.40


ATOM
2475
CB
ASN
A
381
−7.217
88.280
32.701
1.00
69.11


ATOM
2476
CG
ASN
A
381
−8.246
89.240
32.118
1.00
92.46


ATOM
2477
OD1
ASN
A
381
−7.901
90.173
31.391
1.00
84.96


ATOM
2478
ND2
ASN
A
381
−9.516
88.979
32.389
1.00
84.25


ATOM
2479
N
GLN
A
382
−4.173
86.987
31.094
1.00
71.96


ATOM
2480
CA
GLN
A
382
−2.777
86.654
31.338
1.00
76.37


ATOM
2481
C
GLN
A
382
−1.939
86.803
30.067
1.00
97.16


ATOM
2482
O
GLN
A
382
−0.734
86.482
30.101
1.00
97.72


ATOM
2483
CB
GLN
A
382
−2.645
85.233
31.900
1.00
77.20


ATOM
2484
CG
GLN
A
382
−2.538
85.170
33.423
1.00
96.81


ATOM
2485
CD
GLN
A
382
−2.784
83.764
33.984
1.00
117.77


ATOM
2486
OE1
GLN
A
382
−3.602
83.572
34.877
1.00
116.29


ATOM
2487
NE2
GLN
A
382
−2.070
82.788
33.421
1.00
111.31


ATOM
2488
OH
OXY
A
383
−2.483
87.265
29.028
1.00
102.92


ATOM
2489
OW
WAT
W
1
−4.677
75.012
8.897
1.00
29.92


ATOM
2490
OW
WAT
W
2
−2.646
76.265
11.688
1.00
43.10


ATOM
2491
OW
WAT
W
3
−3.542
69.196
−0.989
1.00
25.79


ATOM
2492
OW
WAT
W
4
−14.637
74.665
13.584
1.00
37.39


ATOM
2493
OW
WAT
W
5
−12.047
57.559
7.325
1.00
38.13


ATOM
2494
OW
WAT
W
7
−13.861
59.413
8.131
1.00
37.79


ATOM
2495
OW
WAT
W
9
3.886
72.894
22.594
1.00
44.90


ATOM
2496
OW
WAT
W
10
−7.972
61.813
−0.942
1.00
35.63


ATOM
2497
OW
WAT
W
11
−11.435
56.720
25.315
1.00
46.19


ATOM
2498
OW
WAT
W
12
−5.122
56.927
22.437
1.00
44.04


ATOM
2499
OW
WAT
W
13
−11.727
63.993
26.923
1.00
36.75


ATOM
2500
OW
WAT
W
14
0.335
77.923
32.134
1.00
43.16


ATOM
2501
OW
WAT
W
15
−15.596
65.065
5.230
1.00
45.81


ATOM
2502
OW
WAT
W
17
−13.836
55.971
19.338
1.00
44.33


ATOM
2503
OW
WAT
W
19
6.296
61.088
12.869
1.00
47.22


ATOM
2504
OW
WAT
W
21
−16.352
53.847
28.747
1.00
43.38


ATOM
2505
OW
WAT
W
22
−13.557
86.315
26.448
1.00
43.30


ATOM
2506
OW
WAT
W
23
−9.962
61.079
2.335
1.00
33.74


ATOM
2507
OW
WAT
W
24
0.800
81.118
19.767
1.00
45.67


ATOM
2508
OW
WAT
W
25
−14.545
67.283
24.731
1.00
34.47


ATOM
2509
OW
WAT
W
26
−16.130
69.784
25.742
1.00
36.46


ATOM
2510
OW
WAT
W
27
9.844
66.723
21.240
1.00
53.69


ATOM
2511
OW
WAT
W
28
−2.946
70.139
47.704
1.00
39.92


ATOM
2512
OW
WAT
W
29
4.611
56.076
12.722
1.00
54.38


ATOM
2513
OW
WAT
W
30
−7.608
54.046
20.786
1.00
39.58


ATOM
2514
OW
WAT
W
31
−14.003
64.412
7.297
1.00
37.71


ATOM
2515
OW
WAT
W
33
−12.903
75.723
7.970
1.00
44.47


ATOM
2516
OW
WAT
W
35
−19.004
72.509
22.021
1.00
45.20


ATOM
2517
OW
WAT
W
36
−13.336
82.004
20.014
1.00
37.66


ATOM
2518
OW
WAT
W
38
−0.061
71.463
1.999
1.00
37.04


ATOM
2519
OW
WAT
W
39
−8.643
57.869
24.959
1.00
43.69


ATOM
2520
OW
WAT
W
41
7.283
70.928
27.903
1.00
43.53


ATOM
2521
OW
WAT
W
43
−16.400
53.830
13.182
1.00
41.38


ATOM
2522
OW
WAT
W
44
5.463
73.319
6.228
1.00
54.69


ATOM
2523
OW
WAT
W
45
7.692
75.328
24.020
1.00
43.18


ATOM
2524
OW
WAT
W
47
−18.307
68.157
22.750
1.00
42.43


ATOM
2525
OW
WAT
W
48
−2.078
57.184
4.813
1.00
45.19


ATOM
2526
OW
WAT
W
49
6.108
55.206
7.090
1.00
66.19


ATOM
2527
OW
WAT
W
51
9.568
73.890
24.843
1.00
49.20


ATOM
2528
OW
WAT
W
52
−3.328
49.531
16.566
1.00
62.04


ATOM
2529
OW
WAT
W
54
−16.516
66.659
1.082
1.00
48.24


ATOM
2530
OW
WAT
W
55
−7.652
55.380
23.236
1.00
50.26


ATOM
2531
OW
WAT
W
56
−20.024
65.688
11.384
1.00
72.50


ATOM
2532
OW
WAT
W
57
−9.925
76.205
30.057
1.00
54.47


ATOM
2533
OW
WAT
W
58
−1.233
64.940
1.639
1.00
42.66


ATOM
2534
OW
WAT
W
61
−10.892
50.466
6.274
1.00
48.29


ATOM
2535
OW
WAT
W
65
9.299
61.484
41.958
1.00
46.44


ATOM
2536
OW
WAT
W
67
−20.065
61.496
10.613
1.00
55.80


ATOM
2537
OW
WAT
W
69
−23.666
49.910
8.247
1.00
86.15


ATOM
2538
OW
WAT
W
70
7.604
62.554
8.540
1.00
47.98


ATOM
2539
OW
WAT
W
71
−16.205
68.309
45.189
1.00
81.66


ATOM
2540
OW
WAT
W
501
−6.848
61.106
32.328
1.00
34.79


ATOM
2541
OW
WAT
W
502
−6.056
65.611
32.053
1.00
44.95


ATOM
2542
OW
WAT
W
504
−12.609
65.934
33.134
1.00
54.08


ATOM
2543
OW
WAT
W
505
−0.492
58.965
33.916
1.00
60.61


ATOM
2544
OW
WAT
W
506
1.663
60.618
31.895
1.00
41.18


ATOM
2545
OW
WAT
W
901
−18.586
78.319
18.429
1.00
60.92


ATOM
2546
OW
WAT
W
902
−20.581
76.915
18.100
1.00
33.96


ATOM
2547
OW
WAT
W
903
−7.654
66.937
−0.440
1.00
30.48


ATOM
2548
OW
WAT
W
904
−4.986
66.790
0.007
1.00
41.90


ATOM
2549
PG
AGS
Z
2
−10.329
60.690
33.363
1.00
79.15


ATOM
2550
S1G
AGS
Z
2
−11.702
59.734
33.241
1.00
83.90


ATOM
2551
O2G
AGS
Z
2
−9.285
60.260
32.335
1.00
78.86


ATOM
2552
O3G
AGS
Z
2
−9.721
60.649
34.846
1.00
79.35


ATOM
2553
PB
AGS
Z
2
−9.901
63.477
32.944
1.00
62.99


ATOM
2554
O1B
AGS
Z
2
−8.660
63.229
32.106
1.00
60.14


ATOM
2555
O2B
AGS
Z
2
−10.664
64.619
32.336
1.00
62.79


ATOM
2556
O3B
AGS
Z
2
−10.803
62.183
33.069
1.00
71.46


ATOM
2557
PA
AGS
Z
2
−8.122
64.094
35.161
1.00
55.72


ATOM
2558
O1A
AGS
Z
2
−8.066
63.574
36.566
1.00
55.06


ATOM
2559
O2A
AGS
Z
2
−6.946
63.541
34.424
1.00
54.80


ATOM
2560
O3A
AGS
Z
2
−9.521
63.850
34.465
1.00
60.13


ATOM
2561
O5*
AGS
Z
2
−7.974
65.663
35.192
1.00
52.60


ATOM
2562
C5*
AGS
Z
2
−9.160
66.468
35.413
1.00
50.53


ATOM
2563
C4*
AGS
Z
2
−8.904
67.803
34.746
1.00
48.57


ATOM
2564
O4*
AGS
Z
2
−7.772
68.484
35.344
1.00
47.09


ATOM
2565
C3*
AGS
Z
2
−8.500
67.740
33.287
1.00
47.90


ATOM
2566
O3*
AGS
Z
2
−9.654
67.478
32.491
1.00
49.04


ATOM
2567
C2*
AGS
Z
2
−7.815
69.108
33.114
1.00
46.21


ATOM
2568
O2*
AGS
Z
2
−8.785
70.121
32.912
1.00
46.76


ATOM
2569
C1*
AGS
Z
2
−7.169
69.382
34.481
1.00
46.52


ATOM
2570
N9
AGS
Z
2
−5.705
69.200
34.508
1.00
45.57


ATOM
2571
C8
AGS
Z
2
−5.001
68.031
34.652
1.00
45.35


ATOM
2572
N7
AGS
Z
2
−3.650
68.191
34.558
1.00
45.65


ATOM
2573
C5
AGS
Z
2
−3.458
69.562
34.374
1.00
44.27


ATOM
2374
C6
AGS
Z
2
−2.272
70.329
34.280
1.00
42.72


ATOM
2575
N6
AGS
Z
2
−1.054
69.951
34.355
1.00
42.71


ATOM
2576
N1
AGS
Z
2
−2.576
71.655
34.070
1.00
41.48


ATOM
2577
C2
AGS
Z
2
−3.839
72.241
34.081
1.00
42.68


ATOM
2578
N3
AGS
Z
2
−4.954
71.541
34.188
1.00
43.81


ATOM
2579
C4
AGS
Z
2
−4.730
70.201
34.367
1.00
44.20


ATOM
2580
MG + 2
MG
Z
3
−6.425
63.318
32.114
1.00
33.19


END


























TABLE 4





Structural Coordinate of MEK1/N35/NKFCdel (corresponding to amino 


acids 24 373 of SEQ ID NO: 2)-Compound 2 Binary Complex.

























ATOM
1
N
GLU
A
38
11.364
65.007
12.944
1.00
94.23


ATOM
2
CA
GLU
A
38
10.260
65.768
13.530
1.00
93.90


ATOM
3
C
GLU
A
38
10.492
66.016
15.019
1.00
96.86


ATOM
4
O
GLU
A
38
9.847
66.874
15.624
1.00
96.19


ATOM
5
CB
GLU
A
38
8.921
65.046
13.311
1.00
95.25


ATOM
6
CG
GLU
A
38
8.976
63.536
13.525
1.00
105.67


ATOM
7
CD
GLU
A
38
9.039
62.756
12.218
1.00
125.88


ATOM
8
OE1
GLU
A
38
8.093
61.990
11.933
1.00
119.76


ATOM
9
OE2
GLU
A
38
10.040
62.901
11.484
1.00
119.54


ATOM
10
N
LEU
A
39
11.423
65.266
15.599
1.00
92.97


ATOM
11
CA
LEU
A
39
11.742
65.411
17.012
1.00
92.61


ATOM
12
C
LEU
A
39
12.810
66.488
17.242
1.00
95.48


ATOM
13
O
LEU
A
39
13.358
66.613
18.340
1.00
94.86


ATOM
14
CB
LEU
A
39
12.169
64.067
17.619
1.00
92.68


ATOM
15
CG
LEU
A
39
11.052
63.020
17.794
1.00
97.37


ATOM
16
CD1
LEU
A
39
11.434
61.961
18.824
1.00
97.35


ATOM
17
CD2
LEU
A
39
9.724
63.685
18.169
1.00
99.83


ATOM
18
N
GLU
A
40
13.081
67.275
16.202
1.00
91.39


ATOM
19
CA
GLU
A
40
14.048
68.367
16.294
1.00
90.84


ATOM
20
C
GLU
A
40
13.477
69.466
17.185
1.00
92.87


ATOM
21
O
GLU
A
40
12.259
69.677
17.221
1.00
92.72


ATOM
22
CB
GLU
A
40
14.351
68.931
14.906
1.00
92.36


ATOM
23
CG
GLU
A
40
15.624
68.391
14.270
1.00
104.94


ATOM
24
CD
GLU
A
40
15.661
68.613
12.765
1.00
128.91


ATOM
25
OE1
GLU
A
40
14.680
69.164
12.217
1.00
124.65


ATOM
26
OE2
GLU
A
40
16.668
68.230
12.128
1.00
123.86


ATOM
27
N
LEU
A
41
14.350
70.163
17.906
1.00
87.25


ATOM
28
CA
LEU
A
41
13.908
71.211
18.814
1.00
85.95


ATOM
29
C
LEU
A
41
14.212
72.622
18.327
1.00
87.43


ATOM
30
O
LEU
A
41
15.314
72.914
17.863
1.00
86.77


ATOM
31
CB
LEU
A
41
14.494
70.998
20.212
1.00
85.96


ATOM
32
CG
LEU
A
41
13.630
70.231
21.216
1.00
90.53


ATOM
33
CD1
LEU
A
41
13.522
70.994
22.525
1.00
90.64


ATOM
34
CD2
LEU
A
41
12.251
69.953
20.639
1.00
93.18


ATOM
35
N
ASP
A
42
13.225
73.499
18.461
1.00
82.52


ATOM
36
CA
ASP
A
42
13.371
74.899
18.100
1.00
81.55


ATOM
37
C
ASP
A
42
14.330
75.532
19.098
1.00
83.06


ATOM
38
O
ASP
A
42
14.729
74.894
20.073
1.00
82.66


ATOM
39
CB
ASP
A
42
12.011
75.594
18.202
1.00
83.57


ATOM
40
CG
ASP
A
42
11.943
76.863
17.391
1.00
96.67


ATOM
41
OD1
ASP
A
42
11.321
76.837
16.305
1.00
97.42


ATOM
42
OD2
ASP
A
42
12.491
77.894
17.847
1.00
103.75


ATOM
43
N
GLU
A
43
14.677
76.792
18.878
1.00
77.61


ATOM
44
CA
GLU
A
43
15.561
77.492
19.800
1.00
76.42


ATOM
45
C
GLU
A
43
14.814
77.822
21.088
1.00
76.72


ATOM
46
O
GLU
A
43
15.297
77.553
22.186
1.00
75.55


ATOM
47
CB
GLU
A
43
16.105
78.767
19.160
1.00
78.01


ATOM
48
CG
GLU
A
43
17.587
78.702
18.825
1.00
90.32


ATOM
49
CD
GLU
A
43
18.242
80.071
18.804
1.00
117.01


ATOM
50
OE1
GLU
A
43
17.519
81.081
18.959
1.00
117.21


ATOM
51
OE2
GLU
A
43
19.477
80.137
18.629
1.00
111.89


ATOM
52
N
GLN
A
44
13.617
78.383
20.939
1.00
71.40


ATOM
53
CA
GLN
A
44
12.785
78.739
22.078
1.00
70.25


ATOM
54
C
GLN
A
44
12.270
77.487
22.788
1.00
71.92


ATOM
55
O
GLN
A
44
11.991
77.513
23.988
1.00
71.46


ATOM
56
CB
GLN
A
44
11.623
79.627
21.528
1.00
71.50


ATOM
57
CG
GLN
A
44
10.350
79.461
22.426
1.00
85.85


ATOM
58
CD
GLN
A
44
9.188
80.235
21.824
1.00
104.91


ATOM
59
OE1
GLN
A
44
8.380
79.683
21.071
1.00
99.35


ATOM
60
NE2
GLN
A
44
9.113
81.524
22.134
1.00
97.89


ATOM
61
N
GLN
A
45
12.184
76.386
22.046
1.00
66.67


ATOM
62
CA
GLN
A
45
11.733
75.115
22.604
1.00
65.65


ATOM
63
C
GLN
A
45
12.826
74.487
23.456
1.00
68.35


ATOM
64
O
GLN
A
45
12.547
73.829
24.454
1.00
67.99


ATOM
65
CB
GLN
A
45
11.334
74.148
21.486
1.00
66.67


ATOM
66
CG
GLN
A
45
9.931
74.365
20.930
1.00
68.96


ATOM
67
CD
GLN
A
45
9.552
73.324
19.897
1.00
74.35


ATOM
68
OE1
GLN
A
45
10.356
72.962
19.043
1.00
65.88


ATOM
69
NE2
GLN
A
45
8.328
72.820
19.986
1.00
64.85


ATOM
70
N
ARG
A
46
14.073
74.684
23.043
1.00
64.31


ATOM
71
CA
ARG
A
46
15.219
74.147
23.765
1.00
63.64


ATOM
72
C
ARG
A
46
15.477
74.966
25.031
1.00
65.48


ATOM
73
O
ARG
A
46
15.742
74.418
26.101
1.00
64.40


ATOM
74
CB
ARG
A
46
16.456
74.154
22.869
1.00
65.30


ATOM
75
CG
ARG
A
46
17.423
73.019
23.145
1.00
80.39


ATOM
76
CD
ARG
A
46
18.851
73.535
23.296
1.00
94.98


ATOM
77
NE
ARG
A
46
19.195
73.798
24.692
1.00
106.87


ATOM
78
CZ
ARG
A
46
18.970
72.949
25.691
1.00
122.78


ATOM
79
NH1
ARG
A
46
18.391
71.776
25.455
1.00
111.07


ATOM
80
NH2
ARG
A
46
19.321
73.271
26.927
1.00
109.55


ATOM
81
N
LYS
A
47
15.377
76.282
24.904
1.00
61.12


ATOM
82
CA
LYS
A
47
15.567
77.159
26.038
1.00
60.64


ATOM
83
C
LYS
A
47
14.477
76.888
27.079
1.00
64.19


ATOM
84
O
LYS
A
47
14.744
76.878
28.285
1.00
64.40


ATOM
85
CB
LYS
A
47
15.542
78.624
25.591
1.00
63.03


ATOM
86
CG
LYS
A
47
14.479
79.469
26.272
1.00
81.39


ATOM
87
CD
LYS
A
47
13.709
80.313
25.260
1.00
92.21


ATOM
88
CE
LYS
A
47
14.650
80.981
24.261
1.00
103.34


ATOM
89
NZ
LYS
A
47
13.919
81.851
23.289
1.00
111.26


ATOM
90
N
ARG
A
48
13.260
76.630
26.603
1.00
59.35


ATOM
91
CA
ARG
A
48
12.129
76.345
27.485
1.00
58.49


ATOM
92
C
ARG
A
48
12.304
75.016
28.224
1.00
61.47


ATOM
93
O
ARG
A
48
12.088
74.935
29.437
1.00
60.66


ATOM
94
CB
ARG
A
48
10.818
76.349
26.696
1.00
57.92


ATOM
95
CG
ARG
A
48
10.372
77.733
26.259
1.00
66.13


ATOM
96
CD
ARG
A
48
8.863
77.834
26.167
1.00
72.22


ATOM
97
NE
ARG
A
48
8.426
79.164
25.732
1.00
77.69


ATOM
98
CZ
ARG
A
48
7.879
79.424
24.555
1.00
87.14


ATOM
99
NH1
ARG
A
48
7.671
78.444
23.684
1.00
73.31


ATOM
100
NH2
ARG
A
48
7.532
80.663
24.244
1.00
71.30


ATOM
101
N
LEU
A
49
12.705
73.980
27.492
1.00
57.75


ATOM
102
CA
LEU
A
49
12.920
72.665
28.084
1.00
57.68


ATOM
103
C
LEU
A
49
14.015
72.746
29.140
1.00
62.31


ATOM
104
O
LEU
A
49
13.910
72.152
30.212
1.00
62.45


ATOM
105
CB
LEU
A
49
13.311
71.655
27.003
1.00
57.75


ATOM
106
CG
LEU
A
49
12.446
70.395
26.959
1.00
62.42


ATOM
107
CD1
LEU
A
49
11.124
70.547
27.585
1.00
62.42


ATOM
108
CD2
LEU
A
49
12.220
70.060
25.397
1.00
64.85


ATOM
109
N
GLU
A
50
15.062
73.499
28.823
1.00
58.91


ATOM
110
CA
GLU
A
50
16.200
73.692
29.713
1.00
58.46


ATOM
111
C
GLU
A
50
15.763
74.334
31.029
1.00
61.08


ATOM
112
O
GLU
A
50
16.076
73.831
32.111
1.00
60.77


ATOM
113
CB
GLU
A
50
17.234
74.572
29.022
1.00
59.93


ATOM
114
CG
GLU
A
50
18.642
74.447
29.561
1.00
72.13


ATOM
115
CD
GLU
A
50
19.633
75.327
28.795
1.00
93.82


ATOM
116
OE1
GLU
A
50
19.347
75.674
27.622
1.00
77.95


ATOM
117
OE2
GLU
A
50
20.698
75.662
29.361
1.00
91.32


ATOM
118
N
ALA
A
51
15.066
75.463
30.925
1.00
56.30


ATOM
119
CA
ALA
A
51
14.596
76.195
32.102
1.00
55.36


ATOM
120
C
ALA
A
51
13.795
75.312
33.055
1.00
58.33


ATOM
121
O
ALA
A
51
14.013
75.337
34.267
1.00
58.00


ATOM
122
CB
ALA
A
51
13.781
77.400
31.684
1.00
55.91


ATOM
123
N
PHE
A
52
12.873
74.529
32.500
1.00
53.72


ATOM
124
CA
PHE
A
52
12.032
73.645
33.298
1.00
52.48


ATOM
125
C
PHE
A
52
12.851
72.676
34.142
1.00
56.68


ATOM
126
O
PHE
A
52
12.520
72.415
35.304
1.00
56.03


ATOM
127
CB
PHE
A
52
11.076
72.867
32.403
1.00
53.39


ATOM
128
CG
PHE
A
52
10.231
71.870
33.146
1.00
54.05


ATOM
129
CD1
PHE
A
52
9.052
72.266
33.771
1.00
56.50


ATOM
130
CD2
PHE
A
52
10.618
70.541
33.232
1.00
55.13


ATOM
131
CE1
PHE
A
52
8.276
71.356
34.459
1.00
57.04


ATOM
132
CE2
PHE
A
52
9.841
69.622
33.919
1.00
57.84


ATOM
133
CZ
PHE
A
52
8.673
70.030
34.536
1.00
56.08


ATOM
134
N
LEU
A
53
13.907
72.125
33.552
1.00
53.39


ATOM
135
CA
LEU
A
53
14.757
71.175
34.261
1.00
53.28


ATOM
136
C
LEU
A
53
15.527
71.867
35.366
1.00
57.13


ATOM
137
O
LEU
A
53
15.704
71.319
36.451
1.00
56.47


ATOM
138
CB
LEU
A
53
15.717
70.489
33.299
1.00
53.31


ATOM
139
CG
LEU
A
53
15.097
69.346
32.499
1.00
58.13


ATOM
140
CD1
LEU
A
53
15.410
69.498
31.015
1.00
58.26


ATOM
141
CD2
LEU
A
53
15.569
67.999
33.028
1.00
60.20


ATOM
142
N
THR
A
54
15.975
73.086
35.089
1.00
53.82


ATOM
143
CA
THR
A
54
16.700
73.858
36.076
1.00
53.74


ATOM
144
C
THR
A
54
15.802
74.099
37.292
1.00
58.71


ATOM
145
O
THR
A
54
16.240
73.951
38.436
1.00
58.77


ATOM
146
CB
THR
A
54
17.181
75.209
35.501
1.00
59.18


ATOM
147
OG1
THR
A
54
18.087
74.976
34.412
1.00
56.89


ATOM
148
CG2
THR
A
54
17.884
76.021
36.573
1.00
56.46


ATOM
149
N
GLN
A
55
14.537
74.438
37.041
1.00
55.26


ATOM
150
CA
GLN
A
55
13.581
74.676
38.123
1.00
55.19


ATOM
151
C
GLN
A
55
13.315
73.389
38.900
1.00
58.61


ATOM
152
O
GLN
A
55
13.377
73.373
40.128
1.00
58.51


ATOM
153
CB
GLN
A
55
12.260
75.245
37.578
1.00
56.73


ATOM
154
CG
GLN
A
55
12.343
76.696
37.111
1.00
77.43


ATOM
155
CD
GLN
A
55
11.038
77.193
36.483
1.00
101.45


ATOM
156
OE1
GLN
A
55
10.461
76.538
35.606
1.00
96.70


ATOM
157
NE2
GLN
A
55
10.580
78.365
36.921
1.00
94.32


ATOM
158
N
LYS
A
56
13.032
72.315
38.169
1.00
54.63


ATOM
159
CA
LYS
A
56
12.754
71.006
38.762
1.00
54.04


ATOM
160
C
LYS
A
56
13.960
70.483
39.539
1.00
57.91


ATOM
161
O
LYS
A
56
13.820
69.698
40.476
1.00
57.28


ATOM
162
CB
LYS
A
56
12.356
70.012
37.663
1.00
55.84


ATOM
163
CG
LYS
A
56
12.561
68.561
38.020
1.00
61.89


ATOM
164
CD
LYS
A
56
12.204
67.660
36.846
1.00
68.68


ATOM
165
CE
LYS
A
56
11.855
66.242
37.300
1.00
78.41


ATOM
166
NZ
LYS
A
56
11.455
55.385
36.164
1.00
87.30


ATOM
167
N
GLN
A
57
15.144
70.935
39.146
1.00
54.72


ATOM
168
CA
GLN
A
57
16.381
70.534
39.802
1.00
54.47


ATOM
169
C
GLN
A
57
16.442
71.113
41.215
1.00
57.54


ATOM
170
O
GLN
A
57
16.959
70.482
42.133
1.00
57.00


ATOM
171
CB
GLN
A
57
17.588
71.007
38.984
1.00
55.93


ATOM
172
CG
GLN
A
57
18.605
69.917
38.680
1.00
73.68


ATOM
173
CD
GLN
A
57
18.089
68.892
37.683
1.00
98.07


ATOM
174
OE1
GLN
A
57
18.821
67.993
37.268
1.00
95.99


ATOM
175
NE2
GLN
A
57
16.826
69.032
37.289
1.00
89.35


ATOM
176
N
LYS
A
58
15.901
72.318
41.375
1.00
53.77


ATOM
177
CA
LYS
A
58
15.874
72.997
42.667
1.00
53.47


ATOM
178
C
LYS
A
58
14.855
72.372
43.629
1.00
58.59


ATOM
179
O
LYS
A
58
14.914
72.590
44.847
1.00
58.52


ATOM
180
CB
LYS
A
58
15.587
74.482
42.483
1.00
55.07


ATOM
181
CG
LYS
A
58
16.668
75.227
41.729
1.00
66.07


ATOM
182
CD
LYS
A
58
16.223
76.628
41.358
1.00
75.91


ATOM
183
CE
LYS
A
58
17.338
77.391
40.656
1.00
89.42


ATOM
184
NZ
LYS
A
58
17.139
78.869
40.727
1.00
98.43


ATOM
185
N
VAL
A
59
13.926
71.592
43.079
1.00
55.14


ATOM
186
CA
VAL
A
59
12.922
70.917
43.889
1.00
54.75


ATOM
187
C
VAL
A
59
13.515
69.605
44.372
1.00
58.86


ATOM
188
O
VAL
A
59
14.225
68.918
43.628
1.00
59.10


ATOM
189
CB
VAL
A
59
11.645
70.613
43.071
1.00
58.69


ATOM
190
CG1
VAL
A
59
10.804
69.547
43.765
1.00
58.57


ATOM
191
CG2
VAL
A
59
10.835
71.876
42.855
1.00
58.38


ATOM
192
N
GLY
A
60
13.254
69.257
45.617
1.00
54.99


ATOM
193
CA
GLY
A
60
13.793
68.023
46.154
1.00
54.88


ATOM
194
C
GLY
A
60
12.712
66.970
46.227
1.00
59.47


ATOM
195
O
GLY
A
60
11.819
66.916
45.371
1.00
59.50


ATOM
196
N
GLU
A
61
12.784
66.142
47.258
1.00
55.75


ATOM
197
CA
GLU
A
61
11.791
65.109
47.475
1.00
55.67


ATOM
198
C
GLU
A
61
10.453
65.786
47.764
1.00
58.66


ATOM
199
O
GLU
A
61
10.399
66.776
48.498
1.00
58.71


ATOM
200
CB
GLU
A
61
12.208
64.237
48.661
1.00
57.33


ATOM
201
CG
GLU
A
61
11.936
62.757
48.482
1.00
71.09


ATOM
202
CD
GLU
A
61
11.809
62.033
49.810
1.00
96.62


ATOM
203
OE1
GLU
A
61
12.100
62.656
50.854
1.00
87.13


ATOM
204
OE2
GLU
A
61
11.407
60.846
49.811
1.00
94.32


ATOM
205
N
LEU
A
62
9.382
65.274
47.167
1.00
54.05


ATOM
206
CA
LEU
A
62
8.049
65.850
47.363
1.00
53.14


ATOM
207
C
LEU
A
62
7.371
65.228
48.567
1.00
55.67


ATOM
208
O
LEU
A
62
7.486
64.031
48.798
1.00
55.98


ATOM
209
CB
LEU
A
62
7.194
65.666
46.115
1.00
52.97


ATOM
210
CG
LEU
A
62
7.793
66.239
44.834
1.00
57.41


ATOM
211
CD1
LEU
A
62
6.965
65.835
43.620
1.00
57.63


ATOM
212
CD2
LEU
A
62
7.924
67.759
44.932
1.00
59.03


ATOM
213
N
LYS
A
63
6.686
66.050
49.349
1.00
50.53


ATOM
214
CA
LYS
A
63
6.026
65.580
50.552
1.00
49.18


ATOM
215
C
LYS
A
63
4.688
66.258
50.741
1.00
50.71


ATOM
216
O
LYS
A
63
4.559
67.451
50.488
1.00
50.18


ATOM
217
CB
LYS
A
63
6.909
65.840
51.785
1.00
51.62


ATOM
218
CG
LYS
A
63
8.162
64.986
51.836
1.00
66.14


ATOM
219
CD
LYS
A
63
9.210
65.603
52.753
1.00
76.67


ATOM
220
CE
LYS
A
63
10.327
64.611
53.070
1.00
88.55


ATOM
221
NZ
LYS
A
63
10.011
63.761
54.260
1.00
96.98


ATOM
222
N
ASP
A
64
3.697
65.480
51.173
1.00
46.02


ATOM
223
CA
ASP
A
64
2.326
65.958
51.362
1.00
45.18


ATOM
224
C
ASP
A
64
2.242
67.335
52.005
1.00
48.34


ATOM
225
O
ASP
A
64
1.743
68.287
51.397
1.00
47.71


ATOM
226
CB
ASP
A
64
1.487
64.919
52.154
1.00
46.97


ATOM
227
CG
ASP
A
64
0.236
65.529
52.809
1.00
59.80


ATOM
228
OD1
ASP
A
64
−0.680
65.967
52.067
1.00
61.18


ATOM
229
OD2
ASP
A
64
0.143
65.500
54.074
1.00
66.09


ATOM
230
N
ASP
A
65
2.765
67.444
53.218
1.00
44.49


ATOM
231
CA
ASP
A
65
2.693
68.682
53.978
1.00
44.06


ATOM
232
C
ASP
A
65
3.424
69.865
53.334
1.00
46.93


ATOM
233
O
ASP
A
65
3.393
70.970
53.858
1.00
46.21


ATOM
234
CB
ASP
A
65
3.156
68.454
55.423
1.00
46.11


ATOM
235
CG
ASP
A
65
2.314
67.398
56.159
1.00
59.44


ATOM
236
OD1
ASP
A
65
1.291
66.929
55.590
1.00
60.07


ATOM
237
OD2
ASP
A
65
2.672
67.044
57.317
1.00
68.08


ATOM
238
N
ASP
A
66
4.050
69.632
52.179
1.00
43.26


ATOM
239
CA
ASP
A
66
4.777
70.683
51.462
1.00
42.94


ATOM
240
C
ASP
A
66
3.885
71.397
50.454
1.00
47.21


ATOM
241
O
ASP
A
66
4.299
72.367
49.817
1.00
46.53


ATOM
242
CB
ASP
A
66
5.969
70.086
50.718
1.00
44.94


ATOM
243
CG
ASP
A
66
7.184
69.900
51.610
1.00
57.85


ATOM
244
OD1
ASP
A
66
7.164
70.392
52.761
1.00
58.28


ATOM
245
OD2
ASP
A
66
8.165
69.267
51.152
1.00
63.75


ATOM
246
N
PHE
A
67
2.673
70.890
50.284
1.00
44.43


ATOM
247
CA
PHE
A
67
1.762
71.445
49.299
1.00
44.14


ATOM
248
C
PHE
A
67
0.628
72.278
49.867
1.00
49.31


ATOM
249
O
PHE
A
67
0.156
72.052
50.980
1.00
48.04


ATOM
250
CB
PHE
A
67
1.226
70.344
48.374
1.00
45.53


ATOM
251
CG
PHE
A
67
2.268
69.772
47.454
1.00
46.37


ATOM
252
CD1
PHE
A
67
2.655
70.457
46.314
1.00
48.99


ATOM
253
CD2
PHE
A
67
2.897
68.578
47.755
1.00
48.22


ATOM
254
CE1
PHE
A
67
3.628
69.943
45.472
1.00
49.55


ATOM
255
CE2
PHE
A
67
3.877
68.064
46.923
1.00
50.82


ATOM
256
CZ
PHE
A
67
4.240
68.750
45.777
1.00
48.68


ATOM
257
N
GLU
A
68
0.192
73.244
49.072
1.00
47.71


ATOM
258
CA
GLU
A
68
−0.898
74.117
49.441
1.00
48.09


ATOM
259
C
GLU
A
68
−1.886
74.209
48.264
1.00
52.99


ATOM
260
O
GLU
A
68
−1.545
74.716
47.192
1.00
52.26


ATOM
261
CB
GLU
A
68
−0.350
75.504
49.802
1.00
49.48


ATOM
262
CG
GLU
A
68
−1.405
76.540
50.149
1.00
61.32


ATOM
263
CD
GLU
A
68
−0.861
77.962
50.092
1.00
85.36


ATOM
264
OE1
GLU
A
68
0.232
78.207
50.665
1.00
70.92


ATOM
265
OE2
GLU
A
68
−1.510
78.828
49.463
1.00
86.45


ATOM
266
N
LYS
A
69
−3.094
73.685
48.461
1.00
50.54


ATOM
267
CA
LYS
A
69
−4.115
73.721
47.417
1.00
50.65


ATOM
268
C
LYS
A
69
−4.511
75.156
47.044
1.00
55.17


ATOM
269
O
LYS
A
69
−4.681
76.014
47.916
1.00
54.88


ATOM
270
CB
LYS
A
69
−5.347
72.927
47.835
1.00
53.15


ATOM
271
CG
LYS
A
69
−6.540
73.119
46.906
1.00
68.90


ATOM
272
CD
LYS
A
69
−7.514
71.951
47.002
1.00
78.49


ATOM
273
CE
LYS
A
69
−8.902
72.344
46.523
1.00
88.16


ATOM
274
NZ
LYS
A
69
−9.975
71.617
47.262
1.00
96.17


ATOM
275
N
ILE
A
70
−4.643
75.402
45.742
1.00
52.11


ATOM
276
CA
ILE
A
70
−5.017
76.716
45.221
1.00
51.80


ATOM
277
C
ILE
A
70
−6.419
76.553
44.625
1.00
56.97


ATOM
278
O
ILE
A
70
−7.226
77.548
44.826
1.00
57.33


ATOM
279
CB
ILE
A
70
−4.058
77.178
44.114
1.00
54.44


ATOM
280
CG1
ILE
A
70
−2.659
77.407
44.671
1.00
54.38


ATOM
281
CG2
ILE
A
70
−4.576
78.436
43.467
1.00
55.45


ATOM
282
CD1
ILE
A
70
−1.682
77.937
43.655
1.00
57.36


ATOM
283
N
SER
A
71
−6.693
75.589
43.882
1.00
53.92


ATOM
284
CA
SER
A
71
−7.998
75.400
43.268
1.00
53.90


ATOM
285
C
SER
A
71
−8.115
73.998
42.685
1.00
58.70


ATOM
286
O
SER
A
71
−7.170
73.210
42.750
1.00
58.33


ATOM
287
CB
SER
A
71
−8.238
76.447
42.172
1.00
57.07


ATOM
286
OG
SER
A
71
−7.055
76.709
41.431
1.00
64.78


ATOM
289
N
GLU
A
72
−9.281
73.697
42.115
1.00
55.85


ATOM
290
CA
GLU
A
72
−9.538
72.402
41.485
1.00
55.65


ATOM
291
C
GLU
A
72
−9.407
72.564
39.971
1.00
58.89


ATOM
292
O
GLU
A
72
−10.017
73.457
39.385
1.00
58.46


ATOM
293
CB
GLU
A
72
−10.954
71.930
41.819
1.00
57.18


ATOM
294
CG
GLU
A
72
−11.028
70.631
42.599
1.00
69.46


ATOM
295
CD
GLU
A
72
−11.937
70.743
43.816
1.00
92.54


ATOM
296
OE1
GLU
A
72
−12.248
71.885
44.218
1.00
88.61


ATOM
297
OE2
GLU
A
72
−12.337
69.695
44.368
1.00
85.56


ATOM
298
N
LEU
A
73
−8.601
71.713
39.344
1.00
55.26


ATOM
299
CA
LEU
A
73
−8.398
71.784
37.896
1.00
54.72


ATOM
300
C
LEU
A
73
−9.350
70.846
37.176
1.00
59.25


ATOM
301
O
LEU
A
73
−9.514
70.919
25.962
1.00
58.66


ATOM
302
CB
LEU
A
73
−6.957
71.433
37.536
1.00
54.41


ATOM
303
CG
LEU
A
73
−5.902
72.392
38.061
1.00
58.56


ATOM
304
CD1
LEU
A
73
−4.527
72.025
37.525
1.00
58.43


ATOM
305
CD2
LEU
A
73
−6.271
73.816
37.699
1.00
60.21


ATOM
306
N
GLY
A
74
−9.969
69.949
37.933
1.00
56.58


ATOM
307
CA
GLY
A
74
−10.907
69.006
37.363
1.00
56.76


ATOM
308
C
GLY
A
74
−10.561
67.566
37.695
1.00
61.83


ATOM
309
O
GLY
A
74
−9.403
67.225
37.906
1.00
61.23


ATOM
310
N
ALA
A
75
−11.584
66.724
37.736
1.00
60.03


ATOM
311
CA
ALA
A
75
−11.411
65.313
38.008
1.00
60.82


ATOM
312
C
ALA
A
75
−11.135
64.581
36.710
1.00
67.05


ATOM
313
O
ALA
A
75
−11.610
64.989
35.648
1.00
66.64


ATOM
314
CB
ALA
A
75
−12.657
64.752
38.683
1.00
61.56


ATOM
315
N
GLY
A
76
−10.365
63.502
36.795
1.00
65.54


ATOM
316
CA
GLY
A
76
−10.027
62.711
35.615
1.00
65.92


ATOM
317
C
GLY
A
76
−9.202
61.480
35.984
1.00
71.56


ATOM
318
O
GLY
A
76
−8.242
61.567
36.751
1.00
71.14


ATOM
319
N
ASN
A
77
−9.593
60.333
35.437
1.00
69.41


ATOM
320
CA
ASN
A
77
−8.898
59.079
35.678
1.00
69.80


ATOM
321
C
ASN
A
77
−8.721
58.692
37.139
1.00
74.63


ATOM
322
O
ASN
A
77
−7.602
58.625
37.639
1.00
74.74


ATOM
323
CB
ASN
A
77
−7.549
59.045
34.970
1.00
72.17


ATOM
324
CG
ASN
A
77
−7.076
57.635
34.683
1.00
101.57


ATOM
325
OD1
ASN
A
77
−7.861
56.688
34.722
1.00
99.40


ATOM
326
ND2
ASN
A
77
−5.781
57.478
34.419
1.00
93.06


ATOM
327
N
GLY
A
78
−9.825
58.337
37.779
1.00
71.28


ATOM
328
CA
GLY
A
78
−9.793
57.854
39.154
1.00
70.79


ATOM
329
C
GLY
A
78
−9.237
58.843
40.168
1.00
73.23


ATOM
330
O
GLY
A
78
−9.000
58.479
41.323
1.00
73.64


ATOM
331
N
GLY
A
79
−9.048
60.088
39.755
1.00
67.77


ATOM
332
CA
GLY
A
79
−8.522
61.092
40.675
1.00
66.64


ATOM
333
C
GLY
A
79
−8.804
62.523
40.264
1.00
67.63


ATOM
334
O
GLY
A
79
−2.986
62.823
39.082
1.00
67.61


ATOM
335
N
VAL
A
80
−8.827
63.411
41.248
1.00
61.25


ATOM
336
CA
VAL
A
80
−9.053
64.820
41.001
1.00
59.70


ATOM
337
C
VAL
A
80
−7.699
65.488
40.799
1.00
60.81


ATOM
338
O
VAL
A
80
−6.674
64.959
41.230
1.00
60.49


ATOM
339
CB
VAL
A
80
−9.767
65.473
42.189
1.00
63.48


ATOM
340
CG1
VAL
A
80
−10.424
66.781
41.773
1.00
63.34


ATOM
341
CG2
VAL
A
80
−10.793
64.509
42.775
1.00
63.31


ATOM
342
N
VAL
A
81
−7.693
66.623
40.127
1.00
54.51


ATOM
343
CA
VAL
A
81
−6.455
67.362
39.893
1.00
52.88


ATOM
344
C
VAL
A
81
−6.562
68.752
40.492
1.00
55.16


ATOM
345
O
VAL
A
81
−7.511
69.488
40.223
1.00
54.74


ATOM
346
CB
VAL
A
81
−6.111
67.457
38.383
1.00
55.97


ATOM
347
CG1
VAL
A
81
−4.830
68.245
35.169
1.00
55.24


ATOM
348
CG2
VAL
A
81
−5.991
66.070
37.783
1.00
55.66


ATOM
349
N
PHE
A
82
−5.553
69.096
41.330
1.00
50.44


ATOM
350
CA
PHE
A
82
−5.583
70.382
41.997
1.00
49.07


ATOM
351
C
PHE
A
82
−4.430
71.236
41.522
1.00
50.45


ATOM
352
O
PHE
A
82
−3.331
70.737
41.279
1.00
49.51


ATOM
353
CB
PHE
A
82
−5.465
70.183
43.515
1.00
50.81


ATOM
354
CG
PHE
A
82
−6.663
69.536
44.135
1.00
52.89


ATOM
355
CD1
PHE
A
82
−6.702
68.169
44.339
1.00
56.58


ATOM
356
CD2
PHE
A
82
−7.762
70.296
44.517
1.00
55.66


ATOM
357
CE1
PHE
A
82
−7.814
67.566
44.907
1.00
57.77


ATOM
358
CE2
PHE
A
82
−8.870
69.704
45.093
1.00
58.55


ATOM
359
CZ
PHE
A
82
−8.899
68.337
45.287
1.00
56.83


ATOM
360
N
LYS
A
83
−4.677
72.533
41.409
1.00
45.86


ATOM
361
CA
LYS
A
83
−3.614
73.458
41.097
1.00
44.97


ATOM
362
C
LYS
A
83
−3.084
73.806
42.471
1.00
48.98


ATOM
363
O
LYS
A
83
−3.841
74.228
43.350
1.00
48.79


ATOM
364
CB
LYS
A
83
−4.140
74.709
40.399
1.00
46.62


ATOM
365
CG
LYS
A
83
−3.043
75.628
39.908
1.00
50.39


ATOM
366
CD
LYS
A
83
−3.545
77.044
39.741
1.00
58.01


ATOM
367
CE
LYS
A
83
−2.390
78.018
39.665
1.00
70.87


ATOM
368
NZ
LYS
A
83
−2.712
79.203
38.825
1.00
83.70


ATOM
369
N
VAL
A
84
−1.812
73.519
42.695
1.00
44.65


ATOM
370
CA
VAL
A
84
−1.236
73.704
43.996
1.00
44.12


ATOM
371
C
VAL
A
84
0.022
74.530
43.951
1.00
48.26


ATOM
372
O
VAL
A
84
0.561
74.834
42.880
1.00
47.86


ATOM
373
CB
VAL
A
84
−0.881
72.339
44.641
1.00
47.52


ATOM
374
CG1
VAL
A
84
−2.070
71.383
44.579
1.00
46.97


ATOM
375
CG2
VAL
A
84
0.338
71.729
43.951
1.00
47.09


ATOM
376
N
SER
A
85
0.512
74.851
45.136
1.00
44.45


ATOM
377
CA
SER
A
85
1.742
75.588
45.285
1.00
43.97


ATOM
378
C
SER
A
85
2.689
74.747
46.138
1.00
47.30


ATOM
379
O
SER
A
85
2.323
74.310
47.237
1.00
46.66


ATOM
380
CB
SER
A
85
1.470
76.928
45.975
1.00
46.47


ATOM
381
OG
SER
A
85
2.671
77.547
46.378
1.00
52.52


ATOM
382
N
HIS
A
86
3.874
74.471
45.609
1.00
42.95


ATOM
383
CA
HIS
A
86
4.881
73.750
46.389
1.00
44.46


ATOM
384
C
HIS
A
86
5.611
74.808
47.200
1.00
49.29


ATOM
385
O
HIS
A
86
6.519
75.488
46.700
1.00
48.58


ATOM
386
CB
HIS
A
86
5.876
73.028
45.445
1.00
45.24


ATOM
387
CG
HIS
A
86
6.859
72.171
46.181
1.00
48.80


ATOM
388
ND1
HIS
A
86
8.186
72.517
46.329
1.00
50.67


ATOM
389
CD2
HIS
A
86
6.692
71.016
46.868
1.00
50.44


ATOM
390
CE1
HIS
A
86
8.799
71.598
47.053
1.00
49.98


ATOM
391
NE2
HIS
A
86
7.914
70.677
47.394
1.00
50.24


ATOM
392
N
LYS
A
87
5.141
74.996
48.434
1.00
45.79


ATOM
393
CA
LYS
A
87
5.653
76.021
49.348
1.00
45.59


ATOM
394
C
LYS
A
87
7.164
75.262
49.306
1.00
49.96


ATOM
395
O
LYS
A
87
7.624
77.383
49.024
1.00
50.19


ATOM
396
CB
LYS
A
87
5.199
75.733
50.782
1.00
47.74


ATOM
397
CG
LYS
A
87
3.696
75.929
51.013
1.00
60.83


ATOM
398
CD
LYS
A
87
3.050
74.664
51.564
1.00
72.58


ATOM
399
CE
LYS
A
87
2.483
74.690
52.962
1.00
83.13


ATOM
400
NZ
LYS
A
87
3.251
74.147
54.008
1.00
91.12


ATOM
401
N
PRO
A
88
7.932
75.225
49.606
1.00
45.73


ATOM
402
CA
PRO
A
88
5.391
75.345
49.649
1.00
44.96


ATOM
403
C
PRO
A
88
9.985
76.018
48.411
1.00
48.48


ATOM
404
O
PRO
A
88
10.703
77.014
48.522
1.00
48.44


ATOM
405
CB
PRO
A
88
9.859
73.894
49.761
1.00
46.42


ATOM
406
CG
PRO
A
88
6.669
73.146
50.294
1.00
50.61


ATOM
407
CD
PRO
A
88
7.487
73.826
49.707
1.00
45.98


ATOM
408
N
SER
A
89
9.574
75.482
47.236
1.00
44.82


ATOM
409
CA
SER
A
89
10.209
76.014
45.981
1.00
44.38


ATOM
410
C
SER
A
89
9.479
77.268
45.494
1.00
48.20


ATOM
411
O
SER
A
89
10.041
78.072
44.761
1.00
47.64


ATOM
412
CB
SER
A
89
10.175
74.940
44.892
1.00
47.22


ATOM
413
OG
SER
A
89
8.853
74.484
44.680
1.00
54.86


ATOM
414
N
GLY
A
90
8.224
77.418
45.890
1.00
45.16


ATOM
415
CA
GLY
A
90
7.424
78.546
45.447
1.00
45.24


ATOM
416
C
GLY
A
90
6.821
78.234
44.075
1.00
49.99


ATOM
417
O
GLY
A
90
6.099
79.054
43.495
1.00
49.57


ATOM
418
N
LEU
A
91
7.119
77.038
43.567
1.00
46.88


ATOM
419
CA
LEU
A
91
6.607
76.597
42.268
1.00
46.97


ATOM
420
C
LEU
A
91
5.137
76.209
42.330
1.00
50.37


ATOM
421
O
LEU
A
91
4.679
75.626
43.309
1.00
50.04


ATOM
422
CB
LEU
A
91
7.409
75.394
41.748
1.00
47.07


ATOM
423
CG
LEU
A
91
8.880
75.597
41.397
1.00
52.23


ATOM
424
CD1
LEU
A
91
9.636
74.271
41.512
1.00
52.62


ATOM
425
CD2
LEU
A
91
9.026
76.174
40.003
1.00
53.80


ATOM
426
N
VAL
A
92
4.416
76.486
41.250
1.00
46.43


ATOM
427
CA
VAL
A
92
3.021
76.087
41.133
1.00
45.92


ATOM
428
C
VAL
A
92
3.007
74.817
40.285
1.00
48.32


ATOM
429
O
VAL
A
92
3.808
74.681
39.364
1.00
48.27


ATOM
430
CB
VAL
A
92
2.174
77.172
40.428
1.00
49.56


ATOM
431
CG1
VAL
A
92
0.734
76.722
40.293
1.00
49.23


ATOM
432
CG2
VAL
A
92
2.252
78.479
41.190
1.00
49.37


ATOM
433
N
MET
A
93
2.146
73.866
40.639
1.00
42.86


ATOM
434
CA
MET
A
93
2.058
72.618
39.892
1.00
41.36


ATOM
435
C
MET
A
93
0.646
72.078
39.852
1.00
44.48


ATOM
436
O
MET
A
93
−0.265
72.613
40.483
1.00
43.57


ATOM
437
CB
MET
A
93
2.985
71.541
40.478
1.00
43.09


ATOM
438
CG
MET
A
93
4.014
72.036
41.461
1.00
46.22


ATOM
439
SD
MET
A
93
5.038
70.667
42.131
1.00
49.73


ATOM
440
CE
MET
A
93
6.690
71.373
41.941
1.00
46.12


ATOM
441
N
ALA
A
94
0.482
70.994
39.104
1.00
40.99


ATOM
442
CA
ALA
A
94
−0.781
70.290
39.025
1.00
40.45


ATOM
443
C
ALA
A
94
−0.582
69.017
39.821
1.00
43.64


ATOM
444
O
ALA
A
94
0.337
68.245
39.553
1.00
42.58


ATOM
445
CB
ALA
A
94
−1.123
69.960
37.569
1.00
40.89


ATOM
446
N
ARG
A
95
−1.385
68.843
40.855
1.00
41.19


ATOM
447
CA
ARG
A
95
−1.280
67.665
41.695
1.00
41.36


ATOM
448
C
ARG
A
95
−2.446
66.721
41.421
1.00
47.13


ATOM
449
O
ARG
A
95
−3.593
67.037
41.728
1.00
45.98


ATOM
450
CB
ARG
A
95
−1.254
68.059
43.176
1.00
39.82


ATOM
451
CG
ARG
A
95
−0.851
66.921
44.121
1.00
43.88


ATOM
452
CD
ARG
A
95
−0.819
67.394
45.572
1.00
47.54


ATOM
453
NE
ARG
A
95
−0.572
66.294
46.508
1.00
56.35


ATOM
454
CZ
ARG
A
95
−0.716
66.388
47.830
1.00
69.89


ATOM
455
NH1
ARG
A
95
−1.106
67.533
48.381
1.00
55.00


ATOM
456
NH2
ARG
A
95
−0.469
65.339
48.604
1.00
59.52


ATOM
457
N
LYS
A
96
−2.150
65.572
40.827
1.00
45.69


ATOM
458
CA
LYS
A
96
−3.173
64.571
40.567
1.00
46.52


ATOM
459
C
LYS
A
96
−3.224
63.631
41.766
1.00
53.30


ATOM
460
O
LYS
A
96
−2.199
63.094
42.190
1.00
52.73


ATOM
461
CB
LYS
A
96
−2.863
63.787
39.292
1.00
49.08


ATOM
462
CG
LYS
A
96
−3.684
62.501
39.135
1.00
62.35


ATOM
463
CD
LYS
A
96
−3.990
62.208
37.669
1.00
69.15


ATOM
464
CE
LYS
A
96
−5.216
61.199
37.521
1.00
75.56


ATOM
465
NZ
LYS
A
96
−4.842
60.221
36.430
1.00
82.67


ATOM
466
N
LEU
A
97
−4.407
63.478
42.343
1.00
52.14


ATOM
467
CA
LEU
A
97
−4.570
62.636
43.505
1.00
53.33


ATOM
468
C
LEU
A
97
−5.390
61.409
43.187
1.00
60.18


ATOM
469
O
LEU
A
97
−6.534
61.509
42.734
1.00
59.94


ATOM
470
CB
LEU
A
97
−5.214
63.417
44.647
1.00
53.55


ATOM
471
CG
LEU
A
97
−4.417
64.616
45.151
1.00
58.71


ATOM
472
CD1
LEU
A
97
−5.349
65.764
45.496
1.00
58.91


ATOM
473
CD2
LEU
A
97
−3.543
64.229
46.349
1.00
60.65


ATOM
474
N
ILE
A
98
−4.804
60.249
43.439
1.00
58.65


ATOM
475
CA
ILE
A
98
−5.478
58.952
43.200
1.00
59.11


ATOM
476
C
ILE
A
98
−5.635
58.249
44.515
1.00
65.98


ATOM
477
O
ILE
A
98
−4.652
57.794
45.101
1.00
65.00


ATOM
478
CB
ILE
A
98
−4.691
58.117
42.217
1.00
61.75


ATOM
479
CG1
ILE
A
98
−4.490
58.856
40.895
1.00
61.70


ATOM
480
CG2
ILE
A
98
−5.400
56.792
42.002
1.00
62.25


ATOM
481
CD1
ILE
A
98
−3.511
58.189
39.963
1.00
64.71


ATOM
482
N
HIS
A
99
−6.871
58.146
44.992
1.00
65.70


ATOM
483
CA
HIS
A
99
−7.130
57.454
46.241
1.00
67.05


ATOM
484
C
HIS
A
99
−7.105
55.945
46.060
1.00
72.54


ATOM
485
O
HIS
A
99
−7.886
55.386
45.291
1.00
71.73


ATOM
486
CB
HIS
A
99
−8.449
57.892
46.870
1.00
68.33


ATOM
487
CG
HIS
A
99
−8.652
57.363
48.254
1.00
72.32


ATOM
488
ND1
HIS
A
99
−8.549
58.157
49.378
1.00
74.43


ATOM
489
CD2
HIS
A
99
−8.894
56.106
48.702
1.00
74.36


ATOM
490
CE1
HIS
A
99
−8.748
57.417
50.456
1.00
74.02


ATOM
491
NE2
HIS
A
99
−8.954
56.169
50.073
1.00
74.36


ATOM
492
N
LEU
A
100
−6.194
55.294
46.770
1.00
70.70


ATOM
493
CA
LEU
A
100
−6.041
53.855
46.682
1.00
71.48


ATOM
494
C
LEU
A
100
−5.648
53.249
48.027
1.00
77.47


ATOM
495
O
LEU
A
100
−4.872
53.834
48.791
1.00
77.07


ATOM
496
CB
LEU
A
100
−5.002
53.499
45.620
1.00
71.49


ATOM
497
CG
LEU
A
100
−5.525
53.477
44.186
1.00
76.29


ATOM
498
CD1
LEU
A
100
−4.622
52.644
43.287
1.00
76.50


ATOM
499
CD2
LEU
A
100
−6.946
52.944
44.162
1.00
79.04


ATOM
500
N
GLU
A
101
−6.197
52.077
48.316
1.00
75.65


ATOM
501
CA
GLU
A
101
−5.891
51.377
49.552
1.00
76.09


ATOM
502
C
GLU
A
101
−5.114
50.116
49.216
1.00
81.17


ATOM
503
O
GLU
A
101
−5.698
49.071
48.918
1.00
80.95


ATOM
504
CB
GLU
A
101
−7.176
51.035
50.307
1.00
77.49


ATOM
505
CG
GLU
A
101
−8.196
52.166
50.332
1.00
88.88


ATOM
506
CD
GLU
A
101
−7.912
53.188
51.420
1.00
111.88


ATOM
507
OE1
GLU
A
101
−8.263
52.924
52.589
1.00
109.11


ATOM
508
OE2
GLU
A
101
−7.349
54.258
51.103
1.00
105.84


ATOM
509
N
ILE
A
102
−3.791
50.231
49.210
1.00
78.09


ATOM
510
CA
ILE
A
102
−2.939
49.105
48.870
1.00
78.07


ATOM
511
C
ILE
A
102
−1.746
48.972
49.805
1.00
81.90


ATOM
512
O
ILE
A
102
−1.316
49.941
50.429
1.00
81.14


ATOM
513
CB
ILE
A
102
−2.444
49.188
47.416
1.00
81.21


ATOM
514
CG1
ILE
A
102
−3.062
50.396
46.715
1.00
81.67


ATOM
515
CG2
ILE
A
102
−2.791
47.909
46.665
1.00
82.05


ATOM
516
CD1
ILE
A
102
−4.496
50.122
46.283
1.00
89.77


ATOM
517
N
LYS
A
103
−1.225
47.756
49.902
1.00
78.68


ATOM
518
CA
LYS
A
103
−0.085
47.467
50.757
1.00
78.58


ATOM
519
C
LYS
A
103
1.101
48.342
50.381
1.00
82.23


ATOM
520
O
LYS
A
103
1.320
48.633
49.202
1.00
81.81


ATOM
521
CB
LYS
A
103
0.298
45.991
50.630
1.00
81.15


ATOM
522
CG
LYS
A
103
−0.209
45.339
49.348
1.00
93.74


ATOM
523
CD
LYS
A
103
−0.539
43.868
49.562
1.00
102.90


ATOM
524
CE
LYS
A
103
−2.001
43.676
49.937
1.00
111.03


ATOM
525
NZ
LYS
A
103
−2.414
42.255
49.838
1.00
117.15


ATOM
526
N
PRO
A
104
1.863
48.764
51.385
1.00
78.58


ATOM
527
CA
PRO
A
104
3.033
49.604
51.160
1.00
78.14


ATOM
528
C
PRO
A
104
3.945
49.014
50.082
1.00
82.01


ATOM
529
O
PRO
A
104
4.618
49.747
49.355
1.00
81.68


ATOM
530
CB
PRO
A
104
3.737
49.596
52.520
1.00
79.62


ATOM
531
CG
PRO
A
104
3.316
48.323
53.145
1.00
83.91


ATOM
532
CD
PRO
A
104
1.911
48.083
52.592
1.00
79.11


ATOM
533
N
ALA
A
105
3.950
47.689
49.974
1.00
78.30


ATOM
534
CA
ALA
A
105
4.761
47.012
48.965
1.00
77.92


ATOM
535
C
ALA
A
105
4.248
47.372
47.577
1.00
81.15


ATOM
536
O
ALA
A
105
5.017
47.789
46.704
1.00
80.55


ATOM
537
CB
ALA
A
105
4.719
45.502
49.172
1.00
78.72


ATOM
538
N
ILE
A
106
2.939
47.228
47.392
1.00
77.18


ATOM
539
CA
ILE
A
106
2.288
47.541
46.123
1.00
76.81


ATOM
540
C
ILE
A
106
2.524
48.998
45.706
1.00
80.36


ATOM
541
O
ILE
A
105
3.059
49.270
44.626
1.00
79.75


ATOM
542
CB
ILE
A
106
0.768
47.283
46.203
1.00
79.86


ATOM
543
CG1
ILE
A
106
0.434
45.883
45.689
1.00
80.25


ATOM
544
CG2
ILE
A
106
0.005
48.339
45.427
1.00
80.42


ATOM
545
CD1
ILE
A
106
−1.023
45.505
45.845
1.00
87.47


ATOM
546
N
ARG
A
107
2.116
49.930
46.565
1.00
76.49


ATOM
547
CA
ARG
A
107
2.263
51.357
46.287
1.00
75.91


ATOM
548
C
ARG
A
107
3.712
51.746
45.971
1.00
78.71


ATOM
549
O
ARG
A
107
3.973
52.523
45.044
1.00
77.55


ATOM
550
CB
ARG
A
107
1.737
52.188
47.461
1.00
75.59


ATOM
551
CG
ARG
A
107
2.721
52.302
48.611
1.00
86.25


ATOM
552
CD
ARG
A
107
2.186
53.238
49.683
1.00
99.21


ATOM
553
NE
ARG
A
107
3.249
53.678
50.585
1.00
110.98


ATOM
554
CZ
ARG
A
107
3.365
53.282
51.849
1.00
127.14


ATOM
555
NH1
ARG
A
107
2.482
52.437
52.365
1.00
114.16


ATOM
556
NH2
ARG
A
107
4.360
53.738
52.594
1.00
115.38


ATOM
557
N
ASN
A
108
4.646
51.206
46.749
1.00
75.04


ATOM
558
CA
ASN
A
108
6.068
51.506
46.572
1.00
74.59


ATOM
559
C
ASN
A
108
6.590
51.118
45.186
1.00
77.13


ATOM
560
O
ASN
A
108
7.565
51.696
44.697
1.00
76.45


ATOM
561
CB
ASN
A
108
6.896
50.843
47.669
1.00
76.15


ATOM
562
CG
ASN
A
108
6.879
51.631
48.963
1.00
102.33


ATOM
563
OD1
ASN
A
108
7.258
52.802
48.993
1.00
98.66


ATOM
564
ND2
ASN
A
108
6.410
51.004
50.035
1.00
93.82


ATOM
565
N
GLN
A
109
5.934
50.147
44.556
1.00
72.87


ATOM
566
CA
GLN
A
109
6.317
49.714
43.217
1.00
72.24


ATOM
567
C
GLN
A
109
5.777
50.714
42.202
1.00
74.92


ATOM
568
O
GLN
A
109
6.453
51.067
41.234
1.00
74.56


ATOM
569
CB
GLN
A
109
5.759
48.318
42.920
1.00
73.60


ATOM
570
CG
GLN
A
109
6.324
47.681
41.656
1.00
89.98


ATOM
571
CD
GLN
A
109
5.388
46.656
41.052
1.00
113.47


ATOM
572
OE1
GLN
A
109
5.358
45.502
41.475
1.00
111.91


ATOM
573
NE2
GLN
A
109
4.621
47.070
40.049
1.00
105.49


ATOM
574
N
ILE
A
110
4.552
51.171
42.438
1.00
70.19


ATOM
575
CA
ILE
A
110
3.922
52.146
41.569
1.00
69.44


ATOM
576
C
ILE
A
110
4.825
53.363
41.441
1.00
71.94


ATOM
577
O
ILE
A
110
5.197
53.757
40.338
1.00
71.41


ATOM
578
CB
ILE
A
110
2.553
52.586
42.123
1.00
72.43


ATOM
579
CG1
ILE
A
110
1.492
51.524
41.827
1.00
72.62


ATOM
580
CG2
ILE
A
110
2.150
53.941
41.547
1.00
73.13


ATOM
581
CD1
ILE
A
110
0.492
51.336
42.940
1.00
78.25


ATOM
582
N
ILE
A
111
5.193
53.941
42.582
1.00
67.94


ATOM
583
CA
ILE
A
111
6.079
55.102
42.605
1.00
67.36


ATOM
584
C
ILE
A
111
7.337
54.803
41.802
1.00
71.00


ATOM
585
O
ILE
A
111
7.893
55.683
41.139
1.00
70.62


ATOM
586
CB
ILE
A
111
6.462
55.468
44.040
1.00
70.11


ATOM
587
CG1
ILE
A
111
5.232
55.991
44.796
1.00
70.48


ATOM
588
CG2
ILE
A
111
7.545
56.544
44.036
1.00
70.45


ATOM
589
CD1
ILE
A
111
3.979
56.057
43.947
1.00
75.91


ATOM
590
N
ARG
A
112
7.753
53.542
41.833
1.00
67.17


ATOM
591
CA
ARG
A
112
8.917
53.087
41.085
1.00
66.85


ATOM
592
C
ARG
A
112
8.676
53.243
39.585
1.00
69.04


ATOM
593
O
ARG
A
112
9.456
53.890
38.885
1.00
68.61


ATOM
594
CB
ARG
A
112
9.206
51.616
41.405
1.00
68.88


ATOM
595
CG
ARG
A
112
10.144
51.399
42.583
1.00
83.98


ATOM
596
CD
ARG
A
112
10.559
49.942
42.694
1.00
98.85


ATOM
597
NE
ARG
A
112
10.210
49.373
43.993
1.00
114.29


ATOM
598
CZ
ARG
A
112
10.988
48.534
44.671
1.00
135.30


ATOM
599
NH1
ARG
A
112
12.161
48.164
44.174
1.00
125.73


ATOM
600
NH2
ARG
A
112
10.595
48.071
45.852
1.00
124.83


ATOM
601
N
GLU
A
113
7.591
52.636
39.105
1.00
63.88


ATOM
602
CA
GLU
A
113
7.225
52.687
37.687
1.00
62.77


ATOM
603
C
GLU
A
113
7.029
54.120
37.170
1.00
64.58


ATOM
604
O
GLU
A
113
7.385
54.432
36.034
1.00
64.10


ATOM
605
CB
GLU
A
113
5.963
51.841
37.425
1.00
64.01


ATOM
606
CG
GLU
A
113
5.788
50.661
38.378
1.00
73.60


ATOM
607
CD
GLU
A
113
4.785
49.627
37.871
1.00
91.54


ATOM
608
OE1
GLU
A
113
3.618
49.996
37.619
1.00
81.88


ATOM
609
OE2
GLU
A
113
5.160
48.443
37.751
1.00
84.27


ATOM
610
N
LEU
A
114
6.470
54.986
38.011
1.00
59.56


ATOM
611
CA
LEU
A
114
6.233
56.381
37.627
1.00
58.44


ATOM
612
C
LEU
A
114
7.533
57.160
37.470
1.00
61.50


ATOM
613
O
LEU
A
114
7.555
58.231
36.861
1.00
60.77


ATOM
614
CB
LEU
A
114
5.331
57.072
38.646
1.00
58.02


ATOM
615
CG
LEU
A
114
3.929
56.500
38.748
1.00
61.89


ATOM
616
CD1
LEU
A
114
3.261
56.967
40.024
1.00
61.88


ATOM
617
CD2
LEU
A
114
3.125
56.902
37.535
1.00
63.69


ATOM
618
N
GLN
A
115
8.612
56.620
38.032
1.00
57.79


ATOM
619
CA
GLN
A
115
9.923
57.255
37.954
1.00
57.28


ATOM
620
C
GLN
A
115
10.343
57.484
36.510
1.00
60.97


ATOM
621
O
GLN
A
115
11.105
58.399
36.218
1.00
60.67


ATOM
622
CB
GLN
A
115
10.971
56.410
38.678
1.00
58.35


ATOM
623
CG
GLN
A
115
10.774
56.344
40.185
1.00
61.59


ATOM
624
CD
GLN
A
115
10.404
57.590
40.782
1.00
65.34


ATOM
625
OE1
GLN
A
115
11.217
58.618
40.808
1.00
60.79


ATOM
626
NE2
GLN
A
115
9.171
57.806
41.253
1.00
46.06


ATOM
627
N
VAL
A
116
9.830
56.648
35.612
1.00
57.59


ATOM
628
CA
VAL
A
116
10.133
56.744
34.184
1.00
57.53


ATOM
629
C
VAL
A
116
9.812
58.124
33.595
1.00
60.52


ATOM
630
O
VAL
A
116
10.459
58.568
32.646
1.00
59.73


ATOM
631
CB
VAL
A
116
9.361
55.671
33.380
1.00
61.88


ATOM
632
CG1
VAL
A
116
9.608
55.839
31.895
1.00
61.94


ATOM
633
CG2
VAL
A
116
9.762
54.277
33.833
1.00
61.81


ATOM
634
N
LEU
A
117
8.600
58.782
34.158
1.00
56.96


ATOM
635
CA
LEU
A
117
8.358
60.099
33.693
1.00
56.26


ATOM
636
C
LEU
A
117
9.425
61.179
33.815
1.00
59.27


ATOM
637
O
LEU
A
117
9.266
62.276
33.283
1.00
58.67


ATOM
638
CB
LEU
A
117
7.105
60.535
34.449
1.00
56.17


ATOM
639
CG
LEU
A
117
5.840
59.702
34.255
1.00
60.62


ATOM
640
CD1
LEU
A
117
4.801
60.072
35.312
1.00
60.81


ATOM
641
CD2
LEU
A
117
5.281
59.907
32.859
1.00
62.48


ATOM
642
N
HIS
A
118
10.496
60.883
34.539
1.00
56.09


ATOM
643
CA
HIS
A
118
11.576
61.848
34.725
1.00
56.22


ATOM
644
C
HIS
A
118
12.448
61.923
33.478
1.00
62.04


ATOM
645
O
HIS
A
118
13.231
62.861
33.313
1.00
61.83


ATOM
646
CB
HIS
A
118
12.441
61.474
35.942
1.00
56.62


ATOM
647
CG
HIS
A
118
11.865
61.911
37.255
1.00
59.55


ATOM
648
ND1
HIS
A
118
11.368
61.017
38.192
1.00
61.03


ATOM
649
CD2
HIS
A
118
11.725
63.141
37.804
1.00
60.96


ATOM
650
CE1
HIS
A
118
10.959
61.681
39.252
1.00
60.36


ATOM
651
NE2
HIS
A
118
11.158
62.971
39.045
1.00
60.62


ATOM
652
N
GLU
A
119
12.302
60.935
32.597
1.00
59.57


ATOM
653
CA
GLU
A
119
13.081
60.891
31.366
1.00
59.61


ATOM
654
C
GLU
A
119
12.303
61.419
30.164
1.00
63.22


ATOM
655
O
GLU
A
119
12.868
61.604
29.080
1.00
62.78


ATOM
656
CB
GLU
A
119
13.556
59.471
31.086
1.00
61.14


ATOM
657
CG
GLU
A
119
13.647
58.583
32.313
1.00
73.91


ATOM
658
CD
GLU
A
119
14.048
57.162
31.965
1.00
97.57


ATOM
659
OE1
GLU
A
119
15.091
56.988
31.296
1.00
87.98


ATOM
660
OE2
GLU
A
119
13.306
56.222
32.329
1.00
95.04


ATOM
661
N
CYS
A
120
11.004
61.639
30.350
1.00
59.32


ATOM
662
CA
CYS
A
120
10.152
62.134
29.271
1.00
58.90


ATOM
663
C
CYS
A
120
10.294
63.643
29.123
1.00
61.52


ATOM
664
O
CYS
A
120
9.629
64.409
29.818
1.00
61.49


ATOM
665
CB
CYS
A
120
8.694
61.747
29.512
1.00
59.20


ATOM
666
SG
CYS
A
120
8.361
59.961
29.327
1.00
63.29


ATOM
667
N
ASN
A
121
11.181
64.061
28.227
1.00
56.43


ATOM
668
CA
ASN
A
121
11.436
65.474
28.013
1.00
55.45


ATOM
669
C
ASN
A
121
11.159
65.918
26.581
1.00
56.61


ATOM
670
O
ASN
A
121
11.985
65.753
25.685
1.00
55.66


ATOM
671
CB
ASN
A
121
12.850
65.833
28.454
1.00
57.58


ATOM
672
CG
ASN
A
121
13.159
65.324
29.862
1.00
80.43


ATOM
673
OD1
ASN
A
121
12.368
65.522
30.792
1.00
68.34


ATOM
674
ND2
ASN
A
121
14.264
64.589
30.000
1.00
73.80


ATOM
675
N
SER
A
122
9.973
66.476
26.381
1.00
51.46


ATOM
676
CA
SER
A
122
9.535
66.919
25.069
1.00
49.97


ATOM
677
C
SER
A
122
8.631
68.135
25.228
1.00
51.71


ATOM
678
O
SER
A
122
7.915
68.261
26.213
1.00
51.38


ATOM
679
CB
SER
A
122
8.767
65.785
24.373
1.00
52.53


ATOM
680
OG
SER
A
122
8.024
66.262
23.270
1.00
60.26


ATOM
681
N
PRO
A
123
8.678
69.033
24.257
1.00
46.73


ATOM
682
CA
PRO
A
123
7.844
70.228
24.283
1.00
45.59


ATOM
683
C
PRO
A
123
6.368
69.851
24.141
1.00
47.56


ATOM
684
O
PRO
A
123
5.486
70.693
24.277
1.00
46.81


ATOM
685
CB
PRO
A
123
8.289
70.985
23.025
1.00
47.30


ATOM
686
CG
PRO
A
123
9.656
70.490
22.741
1.00
51.79


ATOM
687
CD
PRO
A
123
9.677
69.069
23.177
1.00
47.18


ATOM
688
N
TYR
A
124
6.120
68.580
23.839
1.00
43.10


ATOM
689
CA
TYR
A
124
4.778
68.087
23.575
1.00
42.60


ATOM
690
C
TYR
A
124
4.270
67.125
24.641
1.00
47.27


ATOM
691
O
TYR
A
124
3.251
66.433
24.455
1.00
46.75


ATOM
692
CB
TYR
A
124
4.743
67.440
22.191
1.00
43.35


ATOM
693
CG
TYR
A
124
5.336
68.330
21.114
1.00
44.58


ATOM
694
CD1
TYR
A
124
4.694
69.497
20.731
1.00
46.09


ATOM
695
CD2
TYR
A
124
6.576
68.045
20.546
1.00
45.28


ATOM
696
CE1
TYR
A
124
5.235
70.336
19.784
1.00
46.86


ATOM
697
CE2
TYR
A
124
7.127
68.873
19.585
1.00
46.29


ATOM
698
CZ
TYR
A
124
6.451
70.030
19.214
1.00
55.18


ATOM
699
OH
TYR
A
124
6.979
70.878
18.255
1.00
56.84


ATOM
700
N
ILE
A
125
4.973
67.099
25.768
1.00
43.66


ATOM
701
CA
ILE
A
125
4.615
66.257
26.892
1.00
43.27


ATOM
702
C
ILE
A
125
4.682
67.135
28.118
1.00
48.08


ATOM
703
O
ILE
A
125
5.611
67.924
28.262
1.00
47.58


ATOM
704
CB
ILE
A
125
5.614
65.100
27.052
1.00
46.34


ATOM
705
CG1
ILE
A
125
5.741
64.310
25.717
1.00
46.42


ATOM
706
CG2
ILE
A
125
5.213
64.195
28.213
1.00
47.09


ATOM
707
CD1
ILE
A
125
4.474
63.597
25.325
1.00
49.13


ATOM
708
N
VAL
A
126
3.671
67.053
28.974
1.00
45.58


ATOM
709
CA
VAL
A
126
3.628
67.895
30.172
1.00
45.60


ATOM
710
C
VAL
A
126
4.800
67.597
31.106
1.00
48.93


ATOM
711
O
VAL
A
126
5.113
66.437
31.370
1.00
48.59


ATOM
712
CB
VAL
A
126
2.298
67.723
30.951
1.00
49.70


ATOM
713
CG1
VAL
A
126
2.020
68.953
31.812
1.00
49.35


ATOM
714
CG2
VAL
A
126
1.150
67.469
29.990
1.00
49.69


ATOM
715
N
GLY
A
127
5.442
68.650
31.607
1.00
45.04


ATOM
716
CA
GLY
A
127
6.563
68.494
32.534
1.00
44.59


ATOM
717
C
GLY
A
127
6.126
67.698
33.761
1.00
48.14


ATOM
718
O
GLY
A
127
5.045
67.916
34.296
1.00
47.02


ATOM
719
N
PHE
A
128
6.969
66.761
34.183
1.00
44.92


ATOM
720
CA
PHE
A
128
6.683
65.914
35.347
1.00
44.18


ATOM
721
C
PHE
A
128
7.670
66.236
36.458
1.00
47.96


ATOM
722
O
PHE
A
128
8.883
66.213
36.248
1.00
47.02


ATOM
723
CB
PHE
A
128
6.799
64.435
34.956
1.00
45.56


ATOM
724
CG
PHE
A
128
6.819
53.484
36.127
1.00
46.80


ATOM
725
CD1
PHE
A
128
5.637
63.082
36.736
1.00
49.68


ATOM
726
CD2
PHE
A
128
8.013
62.923
36.563
1.00
48.71


ATOM
727
CE1
PHE
A
128
5.648
62.175
37.788
1.00
50.48


ATOM
728
CE2
PHE
A
128
8.031
62.011
27.608
1.00
51.55


ATOM
729
CZ
PHE
A
128
6.845
61.642
38.226
1.00
49.63


ATOM
730
N
TYR
A
129
7.150
66.528
37.644
1.00
45.21


ATOM
731
CA
TYR
A
129
8.004
66.848
38.790
1.00
44.90


ATOM
732
C
TYR
A
129
8.361
65.616
39.617
1.00
50.37


ATOM
733
O
TYR
A
129
9.529
65.366
39.899
1.00
50.95


ATOM
734
CB
TYR
A
129
7.349
67.902
39.673
1.00
45.26


ATOM
735
CG
TYR
A
129
7.335
69.272
39.061
1.00
45.91


ATOM
736
CD1
TYR
A
129
8.505
69.993
38.905
1.00
47.70


ATOM
737
CD2
TYR
A
129
6.148
69.844
38.623
1.00
46.34


ATOM
738
CE1
TYR
A
129
8.495
71.251
38.342
1.00
48.02


ATOM
739
CE2
TYR
A
129
6.127
71.099
38.067
1.00
46.97


ATOM
740
CZ
TYR
A
129
7.305
71.799
37.925
1.00
52.51


ATOM
741
OH
TYR
A
129
7.292
73.049
37.354
1.00
51.22


ATOM
742
N
GLY
A
130
7.351
64.854
40.011
1.00
47.11


ATOM
743
CA
GLY
A
130
7.584
63.667
40.813
1.00
46.94


ATOM
744
C
GLY
A
130
6.281
62.996
41.225
1.00
51.61


ATOM
745
O
GLY
A
130
5.192
63.484
40.916
1.00
50.95


ATOM
746
N
ALA
A
131
6.412
61.868
41.924
1.00
49.13


ATOM
747
CA
ALA
A
131
5.278
61.092
42.400
1.00
49.25


ATOM
748
C
ALA
A
131
5.577
60.513
43.784
1.00
53.88


ATOM
749
O
ALA
A
131
6.658
59.962
44.021
1.00
53.41


ATOM
750
CB
ALA
A
131
4.973
59.977
41.432
1.00
50.13


ATOM
751
N
PHE
A
132
4.612
60.628
44.688
1.00
50.29


ATOM
752
CA
PHE
A
132
4.768
60.109
46.037
1.00
50.06


ATOM
753
C
PHE
A
132
3.431
59.604
46.580
1.00
56.60


ATOM
754
O
PHE
A
132
2.373
59.895
46.022
1.00
55.64


ATOM
755
CB
PHE
A
132
5.342
61.190
46.962
1.00
51.11


ATOM
756
CG
PHE
A
132
4.449
62.392
47.123
1.00
51.71


ATOM
757
CD1
PHE
A
132
4.490
63.434
46.205
1.00
54.27


ATOM
758
CD2
PHE
A
132
3.580
62.489
48.198
1.00
52.92


ATOM
759
CE1
PHE
A
132
3.678
64.540
46.353
1.00
54.56


ATOM
760
CE2
PHE
A
132
2.762
63.596
48.351
1.00
55.26


ATOM
761
CZ
PHE
A
132
2.813
64.620
47.432
1.00
53.28


ATOM
762
N
TYR
A
133
3.487
58.850
47.671
1.00
55.63


ATOM
763
CA
TYR
A
133
2.269
58.337
48.279
1.00
56.75


ATOM
764
C
TYR
A
133
2.087
58.911
49.675
1.00
62.10


ATOM
765
O
TYR
A
133
3.066
59.198
50.372
1.00
61.82


ATOM
766
CB
TYR
A
133
2.287
56.819
48.343
1.00
58.47


ATOM
767
CG
TYR
A
133
1.165
56.227
49.154
1.00
60.84


ATOM
768
CD1
TYR
A
133
1.273
56.095
50.528
1.00
62.94


ATOM
769
CD2
TYR
A
133
−0.014
55.830
48.547
1.00
61.83


ATOM
770
CE1
TYR
A
133
0.232
55.574
51.278
1.00
64.17


ATOM
771
CE2
TYR
A
133
−1.047
55.274
49.282
1.00
62.87


ATOM
772
CZ
TYR
A
133
−0.908
55.153
50.653
1.00
71.74


ATOM
773
OH
TYR
A
133
−1.938
54.631
51.392
1.00
74.81


ATOM
774
N
SER
A
134
0.835
59.089
50.079
1.00
59.34


ATOM
775
CA
SER
A
134
0.548
59.549
51.383
1.00
59.42


ATOM
776
C
SER
A
134
−0.900
59.460
51.807
1.00
64.54


ATOM
777
O
SER
A
134
−1.831
59.852
51.102
1.00
63.94


ATOM
778
CB
SER
A
134
0.923
61.127
51.422
1.00
63.01


ATOM
779
OG
SER
A
134
0.414
61.749
52.591
1.00
73.80


ATOM
780
N
ASP
A
135
−1.072
58.874
52.984
1.00
62.30


ATOM
781
CA
ASP
A
135
−2.382
58.648
53.572
1.00
62.36


ATOM
782
C
ASP
A
135
−3.446
58.132
52.602
1.00
66.30


ATOM
783
O
ASP
A
135
−4.475
58.775
52.395
1.00
65.98


ATOM
784
CB
ASP
A
135
−2.862
59.891
54.320
1.00
64.33


ATOM
785
CG
ASP
A
135
−1.980
60.227
55.528
1.00
75.83


ATOM
786
OD1
ASP
A
135
−2.039
61.378
56.016
1.00
76.54


ATOM
787
OD2
ASP
A
135
−1.222
59.337
55.984
1.00
81.57


ATOM
788
N
GLY
A
136
−3.197
56.961
52.030
1.00
62.65


ATOM
789
CA
GLY
A
136
−4.156
56.311
51.150
1.00
62.39


ATOM
790
C
GLY
A
136
−4.377
56.997
49.802
1.00
65.44


ATOM
791
O
GLY
A
136
−5.445
56.868
49.207
1.00
65.38


ATOM
792
N
GLU
A
137
−3.373
57.714
49.312
1.00
60.78


ATOM
793
CA
GLU
A
137
−3.513
58.396
48.025
1.00
59.73


ATOM
794
C
GLU
A
137
−2.191
58.697
47.335
1.00
60.58


ATOM
795
O
GLU
A
137
−1.269
59.244
47.943
1.00
59.90


ATOM
796
CB
GLU
A
137
−4.354
59.676
48.171
1.00
61.23


ATOM
797
CG
GLU
A
137
−3.960
60.559
49.332
1.00
73.26


ATOM
798
CD
GLU
A
137
−4.666
61.901
49.297
1.00
97.17


ATOM
799
OE1
GLU
A
137
−5.670
62.026
48.561
1.00
94.06


ATOM
800
OE2
GLU
A
137
−4.211
62.833
49.996
1.00
90.32


ATOM
801
N
ILE
A
138
−2.109
58.330
46.057
1.00
54.82


ATOM
802
CA
ILE
A
138
−0.915
58.581
45.264
1.00
53.51


ATOM
803
C
ILE
A
138
−0.999
59.962
44.647
1.00
55.50


ATOM
804
O
ILE
A
138
−2.062
60.386
44.192
1.00
55.56


ATOM
805
CB
ILE
A
138
−0.743
57.549
44.132
1.00
56.38


ATOM
806
CG1
ILE
A
138
−0.552
56.141
44.707
1.00
56.83


ATOM
807
CG2
ILE
A
138
0.438
57.918
43.260
1.00
56.56


ATOM
808
CD1
ILE
A
138
0.881
55.805
45.038
1.00
63.27


ATOM
809
N
SER
A
139
0.121
60.665
44.642
1.00
50.00


ATOM
810
CA
SER
A
139
0.171
61.997
44.080
1.00
48.88


ATOM
811
C
SER
A
139
1.138
62.079
42.910
1.00
51.15


ATOM
812
O
SER
A
139
2.311
61.713
43.026
1.00
50.67


ATOM
813
CB
SER
A
139
0.563
63.018
45.153
1.00
52.13


ATOM
814
OG
SER
A
139
−0.580
63.583
45.773
1.00
60.44


ATOM
815
N
ILE
A
140
0.645
62.583
41.788
1.00
46.60


ATOM
816
CA
ILE
A
140
1.474
62.795
40.619
1.00
45.73


ATOM
817
C
ILE
A
140
1.519
64.300
40.381
1.00
48.69


ATOM
818
O
ILE
A
140
0.491
64.938
40.163
1.00
47.62


ATOM
819
CB
ILE
A
140
0.920
62.057
39.376
1.00
48.69


ATOM
820
CG1
ILE
A
140
1.231
60.555
39.471
1.00
49.26


ATOM
821
CG2
ILE
A
140
1.528
62.627
38.103
1.00
48.37


ATOM
822
CD1
ILE
A
140
0.008
59.665
39.458
1.00
52.57


ATOM
823
N
CYS
A
141
2.702
64.874
40.528
1.00
45.88


ATOM
824
CA
CYS
A
141
2.873
66.312
40.389
1.00
45.84


ATOM
825
C
CYS
A
141
3.548
66.643
39.094
1.00
49.16


ATOM
826
O
CYS
A
141
4.581
66.069
38.760
1.00
48.76


ATOM
827
CB
CYS
A
141
3.687
66.869
41.554
1.00
46.19


ATOM
828
SG
CYS
A
141
2.983
66.484
43.180
1.00
50.12


ATOM
829
N
MET
A
142
2.976
67.587
38.364
1.00
45.92


ATOM
830
CA
MET
A
142
3.548
67.976
37.095
1.00
45.84


ATOM
831
C
MET
A
142
3.392
69.433
36.799
1.00
48.14


ATOM
832
O
MET
A
142
2.825
70.193
37.588
1.00
47.40


ATOM
833
CB
MET
A
142
2.947
67.162
35.957
1.00
48.55


ATOM
834
CG
MET
A
142
1.502
66.867
36.109
1.00
52.93


ATOM
835
SD
MET
A
142
1.164
65.166
35.670
1.00
57.75


ATOM
836
CE
MET
A
142
−0.142
64.775
36.869
1.00
54.45


ATOM
837
N
GLU
A
143
3.893
69.813
35.629
1.00
43.87


ATOM
838
CA
GLU
A
143
3.815
71.170
35.168
1.00
43.45


ATOM
839
C
GLU
A
143
2.352
71.600
35.008
1.00
47.32


ATOM
840
O
GLU
A
143
1.520
74.847
34.495
1.00
46.84


ATOM
841
CB
GLU
A
143
4.565
71.286
33.841
1.00
44.56


ATOM
842
CG
GLU
A
143
4.251
72.511
33.040
1.00
51.71


ATOM
843
CD
GLU
A
143
4.739
72.383
31.625
1.00
64.61


ATOM
844
OE1
GLU
A
143
5.218
73.294
31.266
1.00
53.96


ATOM
845
OE2
GLU
A
143
4.659
73.368
30.873
1.00
59.20


ATOM
846
N
HIS
A
144
2.049
72.805
35.480
1.00
44.14


ATOM
847
CA
HIS
A
144
0.705
73.354
35.406
1.00
43.44


ATOM
848
C
HIS
A
144
0.501
74.042
34.058
1.00
46.34


ATOM
849
O
HIS
A
144
1.348
74.811
33.616
1.00
45.77


ATOM
850
CB
HIS
A
144
0.471
74.358
36.568
1.00
43.97


ATOM
851
CG
HIS
A
144
−0.697
75.271
36.354
1.00
47.20


ATOM
852
ND1
HIS
A
144
−2.001
74.871
36.547
1.00
48.77


ATOM
853
CD2
HIS
A
144
−0.758
76.561
35.941
1.00
48.69


ATOM
854
CE1
HIS
A
144
−2.814
75.873
36.267
1.00
48.05


ATOM
855
NE2
HIS
A
144
−2.085
76.908
35.892
1.00
48.34


ATOM
856
N
MET
A
145
−0.606
73.721
33.389
1.00
42.32


ATOM
857
CA
MET
A
145
−0.941
74.313
32.092
1.00
41.53


ATOM
858
C
MET
A
145
−2.172
75.208
32.272
1.00
45.49


ATOM
859
O
MET
A
145
−3.290
74.724
32.519
1.00
44.66


ATOM
860
CB
MET
A
145
−1.204
73.224
31.060
1.00
43.57


ATOM
861
CG
MET
A
145
−0.030
72.294
30.834
1.00
46.88


ATOM
862
SD
MET
A
145
1.285
73.021
29.806
1.00
51.07


ATOM
863
CE
MET
A
145
0.477
73.079
28.185
1.00
47.27


ATOM
864
N
ASP
A
146
−1.947
76.515
32.198
1.00
42.08


ATOM
865
CA
ASP
A
146
−2.982
77.507
32.476
1.00
41.21


ATOM
866
C
ASP
A
146
−4.178
77.547
31.542
1.00
44.17


ATOM
867
O
ASP
A
146
−5.231
78.075
31.903
1.00
43.79


ATOM
868
CB
ASP
A
146
−2.371
78.892
32.644
1.00
42.46


ATOM
869
CG
ASP
A
146
−1.763
79.402
31.380
1.00
51.14


ATOM
870
OD1
ASP
A
146
−1.897
78.718
30.337
1.00
51.56


ATOM
871
OD2
ASP
A
146
−1.175
80.501
31.416
1.00
55.54


ATOM
872
N
GLY
A
147
−4.027
76.993
30.344
1.00
39.86


ATOM
873
CA
GLY
A
147
−5.126
76.968
29.376
1.00
38.73


ATOM
874
C
GLY
A
147
−6.091
75.810
29.660
1.00
40.83


ATOM
875
O
GLY
A
147
−7.227
75.803
29.172
1.00
40.05


ATOM
876
N
GLY
A
148
−5.630
74.837
30.451
1.00
37.02


ATOM
877
CA
GLY
A
148
−6.433
73.656
30.793
1.00
36.77


ATOM
878
C
GLY
A
148
−6.402
72.628
29.653
1.00
40.99


ATOM
879
O
GLY
A
148
−5.504
72.660
28.796
1.00
40.29


ATOM
880
N
SER
A
149
−7.391
71.734
29.634
1.00
37.58


ATOM
881
CA
SER
A
149
−7.489
70.722
28.583
1.00
37.07


ATOM
882
C
SER
A
149
−8.481
71.139
27.477
1.00
40.02


ATOM
883
O
SER
A
149
−9.330
72.015
27.689
1.00
38.94


ATOM
884
CB
SER
A
149
−7.844
69.359
29.168
1.00
40.53


ATOM
885
OG
SER
A
149
−8.816
69.485
30.185
1.00
52.30


ATOM
886
N
LEU
A
150
−8.345
70.527
26.297
1.00
36.51


ATOM
887
CA
LEU
A
150
−9.170
70.878
25.132
1.00
36.41


ATOM
888
C
LEU
A
150
−10.649
70.551
25.269
1.00
40.18


ATOM
889
O
LEU
A
150
−11.498
71.164
24.610
1.00
39.36


ATOM
890
CB
LEU
A
150
−8.577
70.326
23.837
1.00
36.44


ATOM
891
CG
LEU
A
150
−7.318
71.080
23.398
1.00
40.93


ATOM
892
CD1
LEU
A
150
−6.800
70.564
22.069
1.00
41.05


ATOM
893
CD2
LEU
A
150
−7.615
72.563
23.325
1.00
43.05


ATOM
894
N
ASP
A
151
−10.969
69.624
26.157
1.00
36.82


ATOM
895
CA
ASP
A
151
−12.360
69.320
26.426
1.00
36.82


ATOM
896
C
ASP
A
151
−12.979
70.566
27.051
1.00
41.39


ATOM
897
O
ASP
A
151
−14.077
70.965
26.703
1.00
41.56


ATOM
898
CB
ASP
A
151
−12.470
68.142
27.387
1.00
38.67


ATOM
899
CG
ASP
A
151
−11.880
68.439
28.733
1.00
50.99


ATOM
900
OD1
ASP
A
151
−12.448
67.970
29.745
1.00
53.01


ATOM
901
OD2
ASP
A
151
−10.866
69.170
28.789
1.00
56.15


ATOM
902
N
GLN
A
152
−12.225
71.199
27.945
1.00
38.90


ATOM
903
CA
GLN
A
152
−12.657
72.420
28.622
1.00
38.49


ATOM
904
C
GLN
A
152
−12.680
73.594
27.651
1.00
43.22


ATOM
905
O
GLN
A
152
−13.594
74.422
27.685
1.00
43.37


ATOM
906
CB
GLN
A
152
−11.720
72.734
29.805
1.00
39.44


ATOM
907
CG
GLN
A
152
−11.855
71.760
31.000
1.00
50.55


ATOM
908
CD
GLN
A
152
−10.575
71.659
31.884
1.00
67.08


ATOM
909
OE1
GLN
A
152
−9.526
72.250
31.587
1.00
57.19


ATOM
910
NE2
GLN
A
152
−10.679
70.902
32.973
1.00
62.28


ATOM
911
N
VAL
A
153
−11.663
73.674
26.796
1.00
39.66


ATOM
912
CA
VAL
A
153
−11.571
74.760
25.821
1.00
39.45


ATOM
913
C
VAL
A
153
−12.742
74.688
24.838
1.00
43.97


ATOM
914
O
VAL
A
153
−13.355
75.719
24.488
1.00
43.21


ATOM
915
CB
VAL
A
153
−10.237
74.710
25.038
1.00
43.07


ATOM
916
CG1
VAL
A
153
−10.247
75.733
23.898
1.00
42.80


ATOM
917
CG2
VAL
A
153
−9.056
74.952
25.972
1.00
42.56


ATOM
918
N
LEU
A
154
−13.058
73.466
24.407
1.00
40.58


ATOM
919
CA
LEU
A
154
−14.168
73.222
23.491
1.00
40.15


ATOM
920
C
LEU
A
154
−15.482
73.735
24.072
1.00
44.35


ATOM
921
O
LEU
A
154
−16.181
74.527
23.444
1.00
42.94


ATOM
922
CB
LEU
A
154
−14.285
71.729
23.191
1.00
39.93


ATOM
923
CG
LEU
A
154
−15.316
71.333
22.134
1.00
43.73


ATOM
924
CD1
LEU
A
154
−15.186
72.218
20.924
1.00
43.84


ATOM
925
CD2
LEU
A
154
−15.158
69.874
21.755
1.00
44.96


ATOM
926
N
LYS
A
155
−15.809
73.278
25.277
1.00
42.74


ATOM
927
CA
LYS
A
155
−17.039
73.687
25.962
1.00
43.76


ATOM
928
C
LYS
A
155
−17.203
75.197
25.953
1.00
49.78


ATOM
929
O
LYS
A
155
−18.309
75.711
25.822
1.00
49.56


ATOM
930
CB
LYS
A
155
−17.036
73.190
27.410
1.00
46.59


ATOM
931
CG
LYS
A
155
−17.823
71.923
27.638
1.00
60.18


ATOM
932
CD
LYS
A
155
−17.330
71.192
28.872
1.00
72.19


ATOM
933
CE
LYS
A
155
−17.002
72.160
29.998
1.00
87.61


ATOM
934
NZ
LYS
A
155
−15.823
71.708
30.799
1.00
99.56


ATOM
935
N
LYS
A
156
−16.086
75.504
26.102
1.00
47.45


ATOM
936
CA
LYS
A
156
−16.088
77.367
26.124
1.00
46.99


ATOM
937
C
LYS
A
156
−16.226
77.971
24.727
1.00
50.79


ATOM
938
O
LYS
A
156
−17.044
78.854
24.508
1.00
51.46


ATOM
939
CB
LYS
A
156
−14.817
77.888
26.801
1.00
49.12


ATOM
940
CG
LYS
A
156
−14.937
79.291
27.352
1.00
66.39


ATOM
941
CD
LYS
A
156
−14.372
79.390
28.767
1.00
76.30


ATOM
942
CE
LYS
A
156
−14.184
80.846
29.181
1.00
90.65


ATOM
943
NZ
LYS
A
156
−13.810
80.991
30.620
1.00
101.26


ATOM
944
N
ALA
A
157
−15.414
77.490
23.786
1.00
45.87


ATOM
945
CA
ALA
A
157
−15.418
78.002
22.114
1.00
44.28


ATOM
946
C
ALA
A
157
−16.611
77.538
21.568
1.00
45.76


ATOM
947
O
ALA
A
157
−16.978
78.189
20.587
1.00
45.19


ATOM
948
CB
ALA
A
157
−14.116
77.643
21.721
1.00
44.94


ATOM
949
N
GLY
A
158
−17.193
75.402
21.926
1.00
40.97


ATOM
950
CA
GLY
A
158
−18.308
75.854
21.154
1.00
40.41


ATOM
951
C
GLY
A
158
−17.749
74.947
20.062
1.00
43.51


ATOM
952
O
GLY
A
158
−18.198
73.828
19.882
1.00
43.47


ATOM
953
N
ARG
A
159
−16.747
75.436
19.358
1.00
39.94


ATOM
954
CA
ARG
A
159
−16.074
74.649
18.344
1.00
39.66


ATOM
955
C
ARG
A
159
−14.790
75.331
17.890
1.00
42.70


ATOM
956
O
ARG
A
159
−14.756
76.550
17.703
1.00
43.42


ATOM
957
CB
ARG
A
159
−17.012
74.282
17.182
1.00
39.62


ATOM
958
CG
ARG
A
159
−17.228
75.344
16.137
1.00
43.06


ATOM
959
CD
ARG
A
159
−18.307
74.887
15.137
1.00
47.42


ATOM
960
NE
ARG
A
159
−18.372
75.760
13.964
1.00
54.84


ATOM
961
CZ
ARG
A
159
−19.423
76.508
13.646
1.00
64.12


ATOM
962
NH1
ARG
A
159
−20.507
76.475
14.397
1.00
47.16


ATOM
963
NH2
ARG
A
159
−19.388
77.292
12.576
1.00
51.12


ATOM
964
N
ILE
A
160
−13.716
74.548
17.800
1.00
36.74


ATOM
965
CA
ILE
A
160
−12.390
75.062
17.466
1.00
35.31


ATOM
966
C
ILE
A
160
−12.105
75.172
15.951
1.00
38.20


ATOM
967
O
ILE
A
160
−12.357
74.236
15.184
1.00
37.97


ATOM
968
CB
ILE
A
160
−11.297
74.249
18.217
1.00
37.93


ATOM
969
CG1
ILE
A
160
−11.609
74.249
19.731
1.00
37.66


ATOM
970
CG2
ILE
A
160
−9.907
74.820
17.955
1.00
38.25


ATOM
971
CD1
ILE
A
160
−10.858
73.212
20.536
1.00
37.51


ATOM
972
N
PRO
A
161
−11.622
76.339
15.518
1.00
33.76


ATOM
973
CA
PRO
A
161
−11.355
76.566
14.085
1.00
32.53


ATOM
974
C
PRO
A
161
−10.291
73.616
13.517
1.00
36.91


ATOM
975
O
PRO
A
161
−9.361
75.193
14.228
1.00
36.05


ATOM
976
CB
PRO
A
161
−10.885
78.027
14.024
1.00
33.73


ATOM
977
CG
PRO
A
161
−10.898
78.539
15.462
1.00
38.37


ATOM
978
CD
PRO
A
161
−10.979
77.354
16.365
1.00
33.83


ATOM
979
N
GLU
A
162
−10.464
75.258
12.244
1.00
33.45


ATOM
980
CA
GLU
A
162
−9.569
74.345
11.549
1.00
33.38


ATOM
981
C
GLU
A
162
−8.087
74.688
11.705
1.00
39.00


ATOM
982
O
GLU
A
162
−7.248
73.790
11.924
1.00
38.85


ATOM
983
CB
GLU
A
162
−9.929
74.285
10.073
1.00
34.50


ATOM
984
CG
GLU
A
162
−9.101
73.311
9.279
1.00
43.03


ATOM
985
CD
GLU
A
162
−9.493
73.273
7.811
1.00
54.64


ATOM
986
OE1
GLU
A
162
−10.689
73.492
7.506
1.00
39.72


ATOM
987
OE2
GLU
A
162
−8.606
73.010
6.966
1.00
42.42


ATOM
988
N
GLN
A
163
−7.754
75.974
11.565
1.00
35.24


ATOM
989
CA
GLN
A
163
−6.363
76.403
11.662
1.00
34.76


ATOM
990
C
GLN
A
163
−5.793
76.145
13.027
1.00
38.34


ATOM
991
O
GLN
A
163
−4.610
75.842
13.163
1.00
38.69


ATOM
992
CB
GLN
A
163
−6.199
77.869
11.269
1.00
36.22


ATOM
993
CG
GLN
A
163
−5.979
78.074
9.771
1.00
46.84


ATOM
994
CD
GLN
A
163
−5.502
79.477
9.424
1.00
60.12


ATOM
995
OE1
GLN
A
163
−5.645
80.414
10.212
1.00
52.93


ATOM
996
NE2
GLN
A
163
−4.943
79.627
1.228
1.00
51.04


ATOM
997
N
ILE
A
164
−6.642
76.249
14.047
1.00
34.20


ATOM
998
CA
ILE
A
164
−6.213
75.976
15.417
1.00
33.21


ATOM
999
C
ILE
A
164
−6.030
74.478
15.579
1.00
36.38


ATOM
1000
O
ILE
A
164
−5.093
74.017
16.241
1.00
35.52


ATOM
1001
CB
ILE
A
164
−7.253
76.485
16.462
1.00
35.85


ATOM
1002
CG1
ILE
A
164
−7.194
78.023
16.568
1.00
36.27


ATOM
1003
CG2
ILE
A
164
−7.014
75.840
17.818
1.00
34.36


ATOM
1004
CD1
ILE
A
164
−5.772
78.584
16.754
1.00
34.07


ATOM
1005
N
LEU
A
165
−6.908
73.717
14.937
1.00
32.18


ATOM
1006
CA
LEU
A
165
−6.840
72.266
15.007
1.00
31.78


ATOM
1007
C
LEU
A
165
−5.633
71.746
14.261
1.00
34.01


ATOM
1008
O
LEU
A
165
−5.105
70.699
14.591
1.00
32.99


ATOM
1009
CB
LEU
A
165
−8.140
71.628
14.503
1.00
31.78


ATOM
1010
CG
LEU
A
165
−9.322
72.862
15.447
1.00
35.65


ATOM
1011
CD1
LEU
A
265
−10.596
71.213
14.929
1.00
35.50


ATOM
1012
CD2
LEU
A
165
−8.979
71.367
16.852
1.00
36.71


ATOM
1013
N
GLY
A
166
−5.167
72.520
13.290
1.00
31.50


ATOM
1014
CA
GLY
A
166
−3.965
72.169
12.534
1.00
31.39


ATOM
1015
C
GLY
A
166
−2.769
72.131
13.482
1.00
36.13


ATOM
1016
O
GLY
A
166
−1.977
71.191
13.450
1.00
36.27


ATOM
1017
N
LYS
A
167
−2.664
73.152
14.343
1.00
32.54


ATOM
1018
CA
LYS
A
167
−1.573
73.245
15.330
1.00
32.27


ATOM
1019
C
LYS
A
167
−1.664
72.099
16.351
1.00
36.82


ATOM
1020
O
LYS
A
167
−0.662
71.463
16.682
1.00
37.08


ATOM
1021
CB
LYS
A
167
−1.628
74.593
16.062
1.00
34.17


ATOM
1022
CG
LYS
A
167
−0.608
75.626
15.583
1.00
43.40


ATOM
1023
CD
LYS
A
167
−0.023
75.258
14.224
1.00
52.27


ATOM
1024
CE
LYS
A
167
0.063
76.471
13.307
1.00
62.02


ATOM
1025
NZ
LYS
A
167
1.333
76.494
12.523
1.00
69.77


ATOM
1026
N
VAL
A
168
−2.871
71.841
16.838
1.00
32.92


ATOM
1027
CA
VAL
A
168
−3.093
70.745
17.769
1.00
32.69


ATOM
1028
C
VAL
A
168
−2.638
69.426
17.137
1.00
37.24


ATOM
1029
O
VAL
A
168
−1.912
68.647
17.759
1.00
37.65


ATOM
1030
CB
VAL
A
168
−4.580
70.625
18.149
1.00
36.24


ATOM
1031
CG1
VAL
A
168
−4.805
69.423
19.054
1.00
35.54


ATOM
1032
CG2
VAL
A
168
−5.070
71.918
18.807
1.00
35.94


ATOM
1033
N
SER
A
169
−3.059
69.188
15.896
1.00
33.33


ATOM
1034
CA
SER
A
169
−2.688
67.964
15.179
1.00
32.91


ATOM
1035
C
SER
A
169
−1.165
67.753
15.200
1.00
36.68


ATOM
1036
O
SER
A
169
−0.676
66.679
15.564
1.00
35.19


ATOM
1037
CB
SER
A
169
−3.190
68.019
13.728
1.00
35.58


ATOM
1038
OG
SER
A
169
−4.600
68.122
13.677
1.00
39.39


ATOM
1039
N
ILE
A
170
−0.426
68.787
14.805
1.00
33.78


ATOM
1040
CA
ILE
A
170
1.028
68.723
14.793
1.00
33.70


ATOM
1041
C
ILE
A
170
1.573
68.347
16.176
1.00
38.47


ATOM
1042
O
ILE
A
170
2.486
67.532
16.288
1.00
38.71


ATOM
1043
CB
ILE
A
170
1.646
70.074
14.365
1.00
36.78


ATOM
1044
CG1
ILE
A
170
1.208
70.442
12.941
1.00
36.95


ATOM
1045
CG2
ILE
A
170
3.172
70.028
14.475
1.00
37.27


ATOM
1046
CD1
ILE
A
170
1.516
71.877
12.565
1.00
40.82


ATOM
1047
N
ALA
A
171
1.018
68.953
17.224
1.00
34.95


ATOM
1048
CA
ALA
A
171
1.481
68.693
18.583
1.00
34.51


ATOM
1049
C
ALA
A
171
1.174
67.267
19.022
1.00
38.62


ATOM
1050
O
ALA
A
171
2.024
66.583
19.594
1.00
37.69


ATOM
1051
CB
ALA
A
171
0.894
69.702
19.555
1.00
35.11


ATOM
1052
N
VAL
A
172
−0.035
66.808
18.743
1.00
36.14


ATOM
1053
CA
VAL
A
172
−0.385
65.446
19.103
1.00
36.48


ATOM
1054
C
VAL
A
172
0.463
64.422
18.334
1.00
42.34


ATOM
1055
O
VAL
A
172
0.902
63.426
18.901
1.00
42.60


ATOM
1056
CB
VAL
A
172
−1.878
65.156
18.908
1.00
39.89


ATOM
1057
CG1
VAL
A
172
−2.162
63.676
19.205
1.00
39.47


ATOM
1058
CG2
VAL
A
172
−2.727
66.078
19.821
1.00
39.38


ATOM
1059
N
ILE
A
173
0.703
64.676
17.047
1.00
39.43


ATOM
1060
CA
ILE
A
173
1.505
63.753
16.248
1.00
39.85


ATOM
1061
C
ILE
A
173
2.940
63.674
16.772
1.00
43.75


ATOM
1062
O
ILE
A
173
3.481
62.583
16.945
1.00
43.05


ATOM
1063
CB
ILE
A
173
1.544
64.131
14.745
1.00
42.95


ATOM
1064
CG1
ILE
A
173
0.223
63.788
14.065
1.00
43.44


ATOM
1065
CG2
ILE
A
173
2.670
63.387
14.047
1.00
43.53


ATOM
1066
CD1
ILE
A
173
0.061
64.447
12.704
1.00
50.79


ATOM
1067
N
LYS
A
174
3.553
64.838
16.996
1.00
39.83


ATOM
1068
CA
LYS
A
174
4.927
64.909
17.497
1.00
39.25


ATOM
1069
C
LYS
A
174
5.041
64.370
18.919
1.00
44.13


ATOM
1070
O
LYS
A
174
6.088
63.862
19.314
1.00
44.16


ATOM
1071
CB
LYS
A
174
5.453
66.337
17.433
1.00
40.42


ATOM
1072
CG
LYS
A
174
5.652
66.853
16.034
1.00
39.99


ATOM
1073
CD
LYS
A
174
6.397
68.167
16.055
1.00
46.57


ATOM
1074
CE
LYS
A
174
6.692
68.652
14.652
1.00
52.59


ATOM
1075
NZ
LYS
A
174
7.494
69.898
14.671
1.00
62.62


ATOM
1076
N
GLY
A
175
3.959
64.466
19.683
1.00
41.41


ATOM
1077
CA
GLY
A
175
3.924
63.967
21.044
1.00
41.15


ATOM
1078
C
GLY
A
175
3.963
62.436
20.996
1.00
45.46


ATOM
1079
O
GLY
A
175
4.770
61.802
21.672
1.00
44.62


ATOM
1080
N
LEU
A
176
3.104
61.851
20.168
1.00
42.77


ATOM
1081
CA
LEU
A
176
3.054
60.401
20.024
1.00
43.20


ATOM
1082
C
LEU
A
176
4.346
59.857
19.403
1.00
49.80


ATOM
1083
O
LEU
A
176
4.766
58.730
19.695
1.00
49.37


ATOM
1084
CB
LEU
A
176
1.860
59.990
19.171
1.00
42.97


ATOM
1085
CG
LEU
A
176
0.466
60.242
19.742
1.00
46.91


ATOM
1086
CD1
LEU
A
176
−0.598
59.981
18.673
1.00
46.81


ATOM
1087
CD2
LEU
A
176
0.225
59.385
20.956
1.00
47.57


ATOM
1088
N
THR
A
177
4.960
60.651
18.529
1.00
47.66


ATOM
1089
CA
THR
A
177
6.194
60.244
17.876
1.00
47.88


ATOM
1090
C
THR
A
177
7.316
60.197
18.898
1.00
53.24


ATOM
1091
O
THR
A
177
8.146
59.293
18.882
1.00
52.88


ATOM
1092
CB
THR
A
177
6.577
61.198
16.732
1.00
54.28


ATOM
1093
OG1
THR
A
177
5.578
61.138
15.707
1.00
55.23


ATOM
1094
CG2
THR
A
177
7.919
60.805
16.135
1.00
50.82


ATOM
1095
N
TYR
A
178
7.316
61.162
19.810
1.00
50.35


ATOM
1096
CA
TYR
A
178
8.326
61.211
20.846
1.00
50.37


ATOM
1097
C
TYR
A
178
8.192
60.027
21.793
1.00
55.61


ATOM
1098
O
TYR
A
178
9.176
59.365
22.117
1.00
55.49


ATOM
1099
CB
TYR
A
178
8.234
62.514
21.640
1.00
51.28


ATOM
1100
CG
TYR
A
178
9.125
62.511
22.860
1.00
52.68


ATOM
1101
CD1
TYR
A
178
8.708
61.926
24.048
1.00
54.76


ATOM
1102
CD2
TYR
A
178
10.414
63.024
22.803
1.00
53.10


ATOM
1103
CE1
TYR
A
178
9.539
61.884
25.155
1.00
55.55


ATOM
1104
CE2
TYR
A
178
11.247
62.987
23.903
1.00
53.82


ATOM
1105
CZ
TYR
A
178
10.803
62.417
25.074
1.00
61.05


ATOM
1106
OH
TYR
A
178
11.625
62.386
26.168
1.00
63.32


ATOM
1107
N
LEU
A
179
6.974
59.786
22.262
1.00
52.84


ATOM
1108
CA
LEU
A
179
6.710
58.695
23.183
1.00
53.03


ATOM
1109
C
LEU
A
179
7.171
57.367
22.609
1.00
60.24


ATOM
1110
O
LEU
A
179
7.776
56.549
23.307
1.00
60.50


ATOM
1111
CB
LEU
A
179
5.230
58.638
23.524
1.00
52.72


ATOM
1112
CG
LEU
A
179
4.790
59.744
24.478
1.00
56.94


ATOM
1113
CD1
LEU
A
179
3.365
59.520
24.966
1.00
57.08


ATOM
1114
CD2
LEU
A
179
5.754
59.828
25.640
1.00
58.57


ATOM
1115
N
ARG
A
180
6.895
57.165
21.328
1.00
58.35


ATOM
1116
CA
ARG
A
180
7.276
55.943
20.644
1.00
59.02


ATOM
1117
C
ARG
A
180
8.797
55.848
20.452
1.00
65.22


ATOM
1118
O
AEG
A
180
9.435
54.898
20.911
1.00
65.19


ATOM
1119
CB
ARG
A
180
6.577
55.872
19.288
1.00
59.33


ATOM
1120
CG
ARG
A
180
6.215
54.480
18.846
1.00
69.79


ATOM
1121
CD
ARG
A
180
6.442
54.306
17.359
1.00
60.95


ATOM
1122
NE
ARG
A
180
6.685
55.581
16.684
1.00
89.63


ATOM
1123
CZ
ARG
A
180
6.693
55.734
15.363
1.00
104.71


ATOM
1124
NH1
ARG
A
160
6.465
54.692
14.575
1.00
93.72


ATOM
1125
NH2
ARG
A
180
6.928
56.928
14.830
1.00
90.85


ATOM
1126
N
GLU
A
181
9.362
56.833
19.759
1.00
62.74


ATOM
1127
CA
GLU
A
181
10.791
56.855
19.454
1.00
63.13


ATOM
1128
C
GLU
A
181
11.689
56.777
20.678
1.00
68.24


ATOM
1129
O
GLU
A
181
12.388
55.787
20.884
1.00
68.02


ATOM
1130
CB
GLU
A
181
11.149
58.098
18.632
1.00
64.54


ATOM
1131
CG
GLU
A
181
10.713
58.035
17.176
1.00
78.49


ATOM
1132
CD
GLU
A
181
10.665
56.613
16.640
1.00
104.09


ATOM
1133
OE1
GLU
A
181
9.594
56.198
16.148
1.00
102.85


ATOM
1134
OE2
GLU
A
181
11.701
55.914
16.708
1.00
100.60


ATOM
1135
N
LYS
A
182
11.699
57.848
21.464
1.00
65.68


ATOM
1136
CA
LYS
A
182
12.565
57.942
22.633
1.00
65.59


ATOM
1137
C
LYS
A
182
12.303
56.940
23.760
1.00
69.72


ATOM
1138
O
LYS
A
182
13.231
56.528
24.446
1.00
69.62


ATOM
1139
CB
LYS
A
182
12.578
59.373
23.185
1.00
68.09


ATOM
1140
CG
LYS
A
182
12.892
60.446
22.141
1.00
81.36


ATOM
1141
CD
LYS
A
182
14.270
60.237
21.528
1.00
91.59


ATOM
1142
CE
LYS
A
182
15.205
61.398
21.847
1.00
102.75


ATOM
1143
NZ
LYS
A
182
16.596
61.144
21.369
1.00
110.60


ATOM
1144
N
HIS
A
183
11.049
56.560
23.969
1.00
66.47


ATOM
1145
CA
HIS
A
183
10.730
55.663
25.078
1.00
66.63


ATOM
1146
C
HIS
A
183
10.041
54.360
24.706
1.00
70.30


ATOM
1147
O
HIS
A
183
9.655
53.589
25.586
1.00
69.38


ATOM
1148
CB
HIS
A
183
9.926
56.406
26.165
1.00
67.67


ATOM
1149
CG
HIS
A
183
10.494
57.744
26.524
1.00
71.22


ATOM
1150
ND1
HIS
A
183
11.335
57.933
27.599
1.00
73.07


ATOM
1151
CD2
HIS
A
183
10.353
58.958
25.939
1.00
73.09


ATOM
1152
CE1
HIS
A
183
11.680
59.207
27.669
1.00
72.55


ATOM
1153
NE2
HIS
A
183
11.098
59.851
26.673
1.00
72.92


ATOM
1154
N
LYS
A
184
9.907
54.107
23.407
1.00
67.53


ATOM
1155
CA
LYS
A
184
9.272
52.884
22.916
1.00
67.33


ATOM
1156
C
LYS
A
184
7.948
52.610
23.622
1.00
71.45


ATOM
1157
O
LYS
A
184
7.712
51.508
24.119
1.00
71.01


ATOM
1158
CB
LYS
A
184
10.213
51.686
23.066
1.00
69.82


ATOM
1159
CG
LYS
A
184
11.250
51.564
21.951
1.00
83.92


ATOM
1160
CD
LYS
A
184
12.000
50.237
22.031
1.00
94.31


ATOM
1161
CE
LYS
A
184
12.630
49.870
20.689
1.00
105.69


ATOM
1162
NZ
LYS
A
184
12.849
48.401
20.549
1.00
112.90


ATOM
1163
N
ILE
A
185
7.099
53.630
23.685
1.00
68.17


ATOM
1164
CA
ILE
A
185
5.792
53.497
24.317
1.00
67.69


ATOM
1165
C
ILE
A
185
4.742
54.343
23.612
1.00
70.55


ATOM
1166
O
ILE
A
185
5.070
55.275
22.880
1.00
69.96


ATOM
1167
CB
ILE
A
185
5.834
53.838
25.814
1.00
70.63


ATOM
1168
CG1
ILE
A
185
6.168
55.318
26.020
1.00
70.85


ATOM
1169
CG2
ILE
A
185
6.833
52.939
26.533
1.00
71.29


ATOM
1170
CD1
ILE
A
185
6.191
55.740
27.477
1.00
75.31


ATOM
1171
N
MET
A
186
3.480
53.976
23.804
1.00
66.38


ATOM
1172
CA
MET
A
186
2.372
54.677
23.180
1.00
65.69


ATOM
1173
C
MET
A
186
1.501
55.294
24.254
1.00
66.55


ATOM
1174
O
MET
A
186
1.494
54.834
25.397
1.00
66.44


ATOM
1175
CB
MET
A
186
1.547
53.710
22.336
1.00
68.43


ATOM
1176
CG
MET
A
186
0.526
52.920
23.130
1.00
72.60


ATOM
1177
SD
MET
A
186
−0.376
51.753
22.104
1.00
77.44


ATOM
1178
CE
MET
A
186
−2.052
52.517
22.103
1.00
74.17


ATOM
1179
N
HIS
A
187
0.768
56.339
23.891
1.00
60.23


ATOM
1180
CA
HIS
A
187
−0.098
57.014
24.846
1.00
58.75


ATOM
1181
C
HIS
A
187
−1.161
56.084
25.416
1.00
60.40


ATOM
1182
O
HIS
A
187
−1.222
55.875
26.623
1.00
59.98


ATOM
1183
CB
HIS
A
187
−0.757
58.247
24.215
1.00
59.04


ATOM
1184
CG
HIS
A
187
−1.385
59.164
23.214
1.00
61.90


ATOM
1185
ND1
HIS
A
187
−2.642
58.948
25.732
1.00
63.48


ATOM
1186
CD2
HIS
A
187
−0.914
60.279
25.817
1.00
63.38


ATOM
1187
CE1
HIS
A
187
−2.930
59.907
26.594
1.00
62.84


ATOM
1188
NE2
HIS
A
187
−1.896
60.727
26.666
1.00
63.08


ATOM
1189
N
ARG
A
188
−2.010
55.561
24.531
1.00
55.48


ATOM
1190
CA
ARG
A
188
−3.090
54.633
24.895
1.00
54.18


ATOM
1191
C
ARG
A
188
−4.357
55.316
25.386
1.00
54.87


ATOM
1192
O
ARG
A
188
−5.352
54.649
25.572
1.00
54.92


ATOM
1193
CB
ARG
A
188
−2.617
53.583
25.910
1.00
54.64


ATOM
1194
CG
ARG
A
188
−2.287
52.233
25.302
1.00
65.91


ATOM
1195
CD
ARG
A
188
−1.768
51.269
26.354
1.00
76.71


ATOM
1196
NE
ARG
A
188
−0.308
51.279
26.434
1.00
84.42


ATOM
1197
CZ
ARG
A
188
0.476
50.333
25.924
1.00
94.98


ATOM
1198
NH1
ARG
A
188
−0.058
49.296
25.291
1.00
77.49


ATOM
1199
NH2
ARG
A
188
1.793
50.431
26.040
1.00
81.92


ATOM
1200
N
ASP
A
189
−4.325
56.639
25.501
1.00
48.56


ATOM
1201
CA
ASP
A
189
−5.495
57.376
25.966
1.00
47.20


ATOM
1202
C
ASP
A
189
−5.584
58.801
25.428
1.00
48.88


ATOM
1203
O
ASP
A
189
−5.696
59.760
26.191
1.00
47.81


ATOM
1204
CB
ASP
A
189
−5.585
57.368
27.490
1.00
48.73


ATOM
1205
CG
ASP
A
189
−6.980
57.743
27.998
1.00
58.39


ATOM
1206
OD1
ASP
A
189
−7.965
57.571
27.242
1.00
57.97


ATOM
1207
OD2
ASP
A
189
−7.085
58.202
29.159
1.00
66.51


ATOM
1208
N
VAL
A
190
−5.561
58.927
24.106
1.00
44.12


ATOM
1209
CA
VAL
A
190
−5.701
60.220
23.466
1.00
42.91


ATOM
1210
C
VAL
A
190
−7.176
60.633
23.477
1.00
45.01


ATOM
1211
O
VAL
A
190
−8.048
59.857
23.112
1.00
44.16


ATOM
1212
CB
VAL
A
190
−5.199
60.186
22.002
1.00
46.39


ATOM
1213
CG1
VAL
A
190
−5.526
61.502
21.283
1.00
45.99


ATOM
1214
CG2
VAL
A
190
−3.712
59.883
21.950
1.00
45.93


ATOM
1215
N
LYS
A
191
−7.432
61.852
23.936
1.00
41.14


ATOM
1216
CA
LYS
A
191
−8.777
62.433
23.979
1.00
40.25


ATOM
1217
C
LYS
A
191
−8.633
63.898
24.385
1.00
42.77


ATOM
1218
O
LYS
A
191
−7.577
64.308
24.862
1.00
41.69


ATOM
1219
CB
LYS
A
191
−9.676
61.679
24.960
1.00
42.19


ATOM
1220
CG
LYS
A
191
−9.079
61.487
26.343
1.00
43.31


ATOM
1221
CD
LYS
A
191
−9.941
60.586
27.182
1.00
43.52


ATOM
1222
CE
LYS
A
191
−9.637
60.744
28.658
1.00
47.27


ATOM
1223
NZ
LYS
A
191
−10.648
60.064
29.511
1.00
49.19


ATOM
1224
N
PRO
A
192
−9.680
64.690
24.167
1.00
39.33


ATOM
1225
CA
PRO
A
192
−9.623
66.135
24.448
1.00
38.46


ATOM
1226
C
PRO
A
192
−9.175
66.496
25.864
1.00
42.26


ATOM
1227
O
PRO
A
192
−8.405
67.442
26.066
1.00
41.65


ATOM
1228
CB
PRO
A
192
−11.062
66.594
24.197
1.00
39.56


ATOM
1229
CG
PRO
A
192
−11.564
65.662
23.164
1.00
43.80


ATOM
1230
CD
PRO
A
192
−10.932
64.315
23.485
1.00
39.42


ATOM
1231
N
SER
A
193
−9.660
65.748
26.841
1.00
38.97


ATOM
1232
CA
SER
A
193
−9.322
66.005
28.234
1.00
38.85


ATOM
1233
C
SER
A
193
−7.874
65.634
28.566
1.00
42.38


ATOM
1234
O
SER
A
193
−7.393
65.912
29.664
1.00
41.39


ATOM
1235
CB
SER
A
193
−10.287
65.265
29.158
1.00
42.60


ATOM
1236
OG
SER
A
193
−9.923
63.904
29.274
1.00
53.68


ATOM
1237
N
ASN
A
194
−7.185
65.002
27.615
1.00
38.83


ATOM
1238
CA
ASN
A
194
−5.786
64.613
27.814
1.00
37.82


ATOM
1239
C
ASN
A
194
−4.831
65.459
26.975
1.00
40.11


ATOM
1240
O
ASN
A
194
−3.630
65.180
26.899
1.00
39.34


ATOM
1241
CB
ASN
A
194
−5.577
63.115
27.590
1.00
35.71


ATOM
1242
CG
ASN
A
194
−5.982
62.293
28.797
1.00
51.10


ATOM
1243
OD1
ASN
A
194
−6.377
62.846
29.824
1.00
45.44


ATOM
1244
ND2
ASN
A
194
−5.934
60.968
28.666
1.00
38.51


ATOM
1245
N
ILE
A
195
−5.368
66.526
26.394
1.00
35.88


ATOM
1246
CA
ILE
A
195
−4.558
67.479
25.648
1.00
35.59


ATOM
1247
C
ILE
A
195
−4.582
68.818
26.369
1.00
39.99


ATOM
1248
O
ILE
A
195
−5.621
69.456
26.482
1.00
39.22


ATOM
1249
CB
ILE
A
195
−5.033
67.657
24.203
1.00
38.13


ATOM
1250
CG1
ILE
A
195
−5.163
66.288
23.523
1.00
38.60


ATOM
1251
CG2
ILE
A
195
−4.054
68.548
23.438
1.00
37.41


ATOM
1252
CD1
ILE
A
195
−5.872
66.326
22.186
1.00
43.43


ATOM
1253
N
LEU
A
196
−3.435
69.210
26.907
1.00
37.22


ATOM
1254
CA
LEU
A
196
−3.340
70.447
27.656
1.00
36.78


ATOM
1255
C
LEU
A
196
−2.729
71.565
26.840
1.00
40.05


ATOM
1256
O
LEU
A
196
−1.895
71.331
25.979
1.00
39.54


ATOM
1257
CB
LEU
A
196
−2.564
70.231
28.951
1.00
36.78


ATOM
1258
CG
LEU
A
196
−3.165
69.189
29.885
1.00
41.49


ATOM
1259
CD1
LEU
A
196
−2.084
68.535
30.723
1.00
41.99


ATOM
1260
CD2
LEU
A
196
−4.196
69.817
30.759
1.00
44.69


ATOM
1261
N
VAL
A
197
−3.182
72.779
27.101
1.00
36.97


ATOM
1262
CA
VAL
A
197
−2.701
73.953
26.388
1.00
36.70


ATOM
1263
C
VAL
A
197
−2.389
75.061
27.395
1.00
39.84


ATOM
1264
O
VAL
A
197
−2.861
75.023
28.535
1.00
38.46


ATOM
1265
CB
VAL
A
197
−3.756
74.460
25.352
1.00
40.27


ATOM
1266
CG1
VAL
A
197
−3.905
73.462
24.222
1.00
40.16


ATOM
1267
CG2
VAL
A
197
−5.103
74.704
26.026
1.00
39.69


ATOM
1268
N
ASN
A
198
−1.568
76.023
26.986
1.00
36.84


ATOM
1269
CA
ASN
A
198
−1.219
77.131
27.869
1.00
37.15


ATOM
1270
C
ASN
A
198
−1.145
78.484
27.152
1.00
43.66


ATOM
1271
O
ASN
A
198
−1.168
78.552
25.916
1.00
42.29


ATOM
1272
CB
ASN
A
198
0.050
76.831
28.718
1.00
33.66


ATOM
1273
CG
ASN
A
198
1.345
76.834
27.892
1.00
45.53


ATOM
1274
OD1
ASN
A
198
1.505
77.616
26.947
1.00
37.29


ATOM
1275
ND2
ASN
A
198
2.299
76.006
28.302
1.00
33.83


ATOM
1276
N
SER
A
199
−1.116
79.559
27.940
1.00
42.82


ATOM
1277
CA
SER
A
199
−1.077
80.910
27.398
1.00
43.39


ATOM
1278
C
SER
A
199
0.160
81.189
26.549
1.00
49.10


ATOM
1279
O
SER
A
199
0.200
82.174
25.810
1.00
49.86


ATOM
1280
CB
SER
A
199
−1.211
81.944
28.511
1.00
47.18


ATOM
1281
OG
SER
A
199
−0.374
81.634
29.606
1.00
56.20


ATOM
1282
N
ARG
A
200
1.163
80.322
26.637
1.00
45.81


ATOM
1283
CA
ARG
A
200
2.365
80.493
25.823
1.00
45.84


ATOM
1284
C
ARG
A
200
2.163
79.920
24.413
1.00
49.34


ATOM
1285
O
ARG
A
200
3.045
80.022
23.561
1.00
49.34


ATOM
1286
CB
ARG
A
200
3.575
79.840
26.491
1.00
47.59


ATOM
1287
CG
ARG
A
200
4.018
80.519
27.765
1.00
61.46


ATOM
1288
CD
ARG
A
200
4.953
79.629
28.552
1.00
81.13


ATOM
1289
NE
ARG
A
200
6.111
80.360
29.056
1.00
98.43


ATOM
1290
CZ
ARG
A
200
7.347
79.874
29.077
1.00
115.62


ATOM
1291
NH1
ARG
A
200
7.586
78.651
28.617
1.00
101.79


ATOM
1292
NH2
ARG
A
200
8.342
80.606
29.557
1.00
104.72


ATOM
1293
N
GLY
A
201
1.000
79.314
24.178
1.00
44.83


ATOM
1294
CA
GLY
A
201
0.676
78.744
22.871
1.00
44.06


ATOM
1295
C
GLY
A
201
1.184
77.309
22.722
1.00
46.16


ATOM
1296
O
GLY
A
201
1.341
76.802
21.600
1.00
46.06


ATOM
1297
N
GLU
A
202
1.433
76.662
23.855
1.00
40.38


ATOM
1298
CA
GLU
A
202
1.943
75.300
23.874
1.00
39.05


ATOM
1299
C
GLU
A
202
0.832
74.252
23.960
1.00
41.82


ATOM
1300
O
GLU
A
202
−0.172
74.439
24.661
1.00
40.92


ATOM
1301
CB
GLU
A
202
2.904
75.112
25.048
1.00
40.09


ATOM
1302
CG
GLU
A
202
4.220
75.852
24.902
1.00
47.45


ATOM
1303
CD
GLU
A
202
5.103
75.706
26.129
1.00
65.03


ATOM
1304
OE1
GLU
A
202
4.598
75.895
27.261
1.00
56.38


ATOM
1305
OE2
GLU
A
202
6.298
75.389
25.962
1.00
58.84


ATOM
1306
N
ILE
A
203
1.053
73.129
23.284
1.00
37.73


ATOM
1307
CA
ILE
A
203
0.115
72.015
23.285
1.00
37.36


ATOM
1308
C
ILE
A
203
0.852
70.755
23.740
1.00
41.58


ATOM
1309
O
ILE
A
203
1.926
70.430
23.213
1.00
41.07


ATOM
1310
CB
ILE
A
243
−0.530
71.814
21.881
1.00
39.94


ATOM
1311
CG1
ILE
A
203
−1.212
73.114
21.436
1.00
39.84


ATOM
1312
CG2
ILE
A
203
−1.558
70.684
21.923
1.00
40.58


ATOM
1313
CD1
ILE
A
203
−1.171
73.356
19.949
1.00
43.22


ATOM
1314
N
LYS
A
204
0.319
70.091
24.765
1.00
38.53


ATOM
1315
CA
LYS
A
204
0.986
68.912
25.341
1.00
38.67


ATOM
1316
C
LYS
A
204
0.059
67.760
25.681
1.00
45.07


ATOM
1317
O
LYS
A
204
−1.112
67.959
26.005
1.00
44.36


ATOM
1318
CB
LYS
A
204
1.786
69.302
26.592
1.00
39.37


ATOM
1319
CG
LYS
A
204
3.067
70.051
26.293
1.00
38.47


ATOM
1320
CD
LYS
A
204
3.440
71.003
27.410
1.00
35.91


ATOM
1321
CE
LYS
A
204
4.833
71.586
27.191
1.00
39.17


ATOM
1322
NZ
LYS
A
204
5.307
72.396
28.350
1.00
42.66


ATOM
1323
N
LEU
A
205
0.607
66.549
25.645
1.00
43.98


ATOM
1324
CA
LEU
A
205
−0.149
65.355
26.006
1.00
44.78


ATOM
1325
C
LEU
A
205
0.104
65.009
27.463
1.00
52.20


ATOM
1326
O
LEU
A
205
1.176
65.286
28.000
1.00
51.40


ATOM
1327
CB
LEU
A
205
0.279
64.167
25.144
1.00
44.64


ATOM
1328
CG
LEU
A
205
0.111
64.238
23.635
1.00
48.60


ATOM
1329
CD1
LEU
A
205
0.581
62.926
23.012
1.00
48.35


ATOM
1330
CD2
LEU
A
205
−1.335
64.527
23.280
1.00
50.23


ATOM
1331
N
CYS
A
206
−0.866
64.351
28.082
1.00
52.50


ATOM
1332
CA
CYS
A
206
−0.727
63.906
29.465
1.00
53.92


ATOM
1333
C
CYS
A
206
−1.528
62.633
29.716
1.00
60.41


ATOM
1334
O
CYS
A
206
−2.328
62.216
28.879
1.00
59.71


ATOM
1335
CB
CYS
A
206
−1.153
65.010
30.441
1.00
54.37


ATOM
1336
SG
CYS
A
206
−2.951
65.314
30.519
1.00
58.54


ATOM
1337
N
ASP
A
207
−1.296
62.020
30.871
1.00
59.87


ATOM
1338
CA
ASP
A
207
−2.008
60.805
31.279
1.00
61.16


ATOM
1339
C
ASP
A
207
−1.808
59.576
30.381
1.00
67.08


ATOM
1340
O
ASP
A
207
−2.762
58.857
30.078
1.00
66.46


ATOM
1341
CB
ASP
A
207
−3.500
61.085
31.514
1.00
63.53


ATOM
1342
CG
ASP
A
207
−3.779
61.669
32.908
1.00
78.02


ATOM
1343
OD1
ASP
A
207
−2.818
62.112
33.580
1.00
78.87


ATOM
1344
OD2
ASP
A
207
−4.961
61.693
33.322
1.00
85.61


ATOM
1345
N
PHE
A
208
−0.559
59.316
30.001
1.00
65.57


ATOM
1346
CA
PHE
A
208
−0.233
58.138
29.203
1.00
66.48


ATOM
1347
C
PHE
A
208
0.328
57.053
30.126
1.00
73.29


ATOM
1348
O
PHE
A
208
1.321
57.272
30.816
1.00
73.06


ATOM
1349
CB
PHE
A
208
0.775
58.476
28.101
1.00
68.15


ATOM
1350
CG
PHE
A
208
1.840
59.446
28.525
1.00
69.60


ATOM
1351
CD1
PHE
A
208
3.015
58.996
29.103
1.00
72.28


ATOM
1352
CD2
PHE
A
208
1.676
60.811
28.321
1.00
71.65


ATOM
1353
CE1
PHE
A
208
3.997
59.883
29.488
1.00
73.10


ATOM
1354
CE2
PHE
A
208
2.653
61.703
28.701
1.00
74.33


ATOM
1355
CZ
PHE
A
208
3.817
61.239
29.288
1.00
72.39


ATOM
1356
N
GLY
A
209
−0.342
55.902
30.157
1.00
71.60


ATOM
1357
CA
GLY
A
209
0.043
54.786
31.025
1.00
72.29


ATOM
1358
C
GLY
A
209
1.548
54.505
31.060
1.00
77.96


ATOM
1359
O
GLY
A
209
2.190
54.354
30.017
1.00
77.94


ATOM
1360
N
VAL
A
210
2.099
54.428
32.269
1.00
75.35


ATOM
1361
CA
VAL
A
210
3.519
54.150
32.453
1.00
75.57


ATOM
1362
C
VAL
A
210
3.722
53.146
33.586
1.00
80.95


ATOM
1363
O
VAL
A
210
4.735
52.449
33.640
1.00
80.43


ATOM
1364
CB
VAL
A
210
4.314
55.436
32.757
1.00
79.27


ATOM
1365
CG1
VAL
A
210
5.746
55.098
33.126
1.00
79.07


ATOM
1366
CG2
VAL
A
210
4.275
56.378
31.566
1.00
78.97


ATOM
1367
N
SER
A
211
2.742
53.072
34.482
1.00
78.75


ATOM
1368
CA
SER
A
211
2.800
52.153
35.611
1.00
79.09


ATOM
1369
C
SER
A
211
1.713
51.081
35.500
1.00
84.05


ATOM
1370
O
SER
A
211
3.530
51.355
35.716
1.00
83.43


ATOM
1371
CB
SER
A
211
2.667
52.915
36.937
1.00
82.77


ATOM
1372
OG
SER
A
211
2.122
52.092
37.960
1.00
91.55


ATOM
1373
N
GLY
A
212
2.119
49.864
35.152
1.00
81.64


ATOM
1374
CA
GLY
A
212
1.182
48.755
35.030
1.00
81.86


ATOM
1375
C
GLY
A
212
0.446
48.551
36.355
1.00
86.67


ATOM
1376
O
GLY
A
212
−0.787
48.503
36.394
1.00
86.31


ATOM
1377
N
GLN
A
213
1.210
48.460
37.441
1.00
83.80


ATOM
1378
CA
GLN
A
213
0.637
48.274
38.769
1.00
83.91


ATOM
1379
C
GLN
A
213
−0.465
49.297
39.060
1.00
88.50


ATOM
1380
O
GLN
A
213
−1.563
48.933
39.492
1.00
88.07


ATOM
1381
CB
GLN
A
213
1.722
48.334
39.844
1.00
85.22


ATOM
1382
CG
GLN
A
213
1.453
47.438
41.060
1.00
98.46


ATOM
1383
CD
GLN
A
213
0.085
46.770
41.005
1.00
114.62


ATOM
1384
OE1
GLN
A
213
−0.948
47.431
41.121
1.00
109.32


ATOM
1385
NE2
GLN
A
213
0.070
45.453
40.888
1.00
106.23


ATOM
1386
N
LEU
A
214
−0.176
50.571
38.813
1.00
85.28


ATOM
1387
CA
LEU
A
214
−1.165
51.619
39.030
1.00
85.25


ATOM
1388
C
LEU
A
214
−2.444
51.285
38.260
1.00
90.51


ATOM
1389
O
LEU
A
214
−3.542
51.300
38.823
1.00
90.20


ATOM
1390
CB
LEU
A
214
−0.619
52.974
38.577
1.00
84.97


ATOM
1391
CG
LEU
A
214
−1.592
54.152
38.677
1.00
88.93


ATOM
1392
CD1
LEU
A
214
−2.240
54.197
40.046
1.00
88.74


ATOM
1393
CD2
LEU
A
214
−0.884
55.463
38.364
1.00
90.67


ATOM
1394
N
ILE
A
215
−2.286
50.967
36.974
1.00
87.75


ATOM
1395
CA
ILE
A
215
−3.418
50.619
36.121
1.00
87.74


ATOM
1396
C
ILE
A
215
−4.260
49.518
36.762
1.00
91.91


ATOM
1397
O
ILE
A
215
−5.484
49.632
36.860
1.00
91.40


ATOM
1398
CB
ILE
A
215
−2.948
50.149
34.725
1.00
90.82


ATOM
1399
CG1
ILE
A
215
−3.080
51.285
33.707
1.00
91.33


ATOM
1400
CG2
ILE
A
215
−3.747
48.934
34.276
1.00
91.15


ATOM
1401
CD1
ILE
A
215
−1.925
51.272
32.726
1.00
98.32


ATOM
1402
N
ASP
A
216
−3.590
48.460
37.211
1.00
88.51


ATOM
1403
CA
ASP
A
216
−4.261
47.333
37.850
1.00
88.33


ATOM
1404
C
ASP
A
216
−5.127
47.783
39.026
1.00
92.07


ATOM
1405
O
ASP
A
216
−6.356
47.693
38.977
1.00
91.70


ATOM
1406
CB
ASP
A
216
−3.235
46.303
38.329
1.00
90.23


ATOM
1407
CG
ASP
A
216
−2.398
45.744
37.196
1.00
100.15


ATOM
1408
OD1
ASP
A
216
−2.773
45.941
36.022
1.00
101.05


ATOM
1409
OD2
ASP
A
216
−1.365
45.096
37.482
1.00
105.09


ATOM
1410
N
SER
A
217
−4.474
48.259
40.084
1.00
88.31


ATOM
1411
CA
SER
A
217
−5.169
48.715
41.283
1.00
87.91


ATOM
1412
C
SER
A
217
−6.168
49.829
40.984
1.00
91.38


ATOM
1413
O
SER
A
217
−7.138
50.021
41.723
1.00
90.84


ATOM
1414
CB
SER
A
217
−4.165
49.178
42.340
1.00
91.22


ATOM
1415
OG
SER
A
217
−2.860
48.700
42.049
1.00
99.33


ATOM
1416
N
MET
A
218
−5.899
50.593
39.930
1.00
87.95


ATOM
1417
CA
GLY
A
224
−12.073
55.924
32.174
1.00
51.00


ATOM
1418
C
GLY
A
224
−12.850
55.606
30.892
1.00
54.54


ATOM
1419
O
GLY
A
224
−12.908
54.455
30.460
1.00
54.03


ATOM
1420
N
THR
A
225
−13.436
56.636
30.285
1.00
50.41


ATOM
1421
CA
THR
A
225
−14.215
56.469
29.063
1.00
49.73


ATOM
1422
C
THR
A
225
−13.470
55.704
27.964
1.00
51.92


ATOM
1423
O
THR
A
225
−12.281
55.928
27.731
1.00
51.83


ATOM
1424
CB
THR
A
225
−14.676
57.820
28.497
1.00
58.66


ATOM
1425
OG1
THR
A
225
−15.947
57.661
27.862
1.00
60.63


ATOM
1426
CG2
THR
A
225
−13.673
58.342
27.476
1.00
56.21


ATOM
1427
N
ARG
A
226
−14.201
54.840
27.261
1.00
46.46


ATOM
1428
CA
ARG
A
226
−13.647
54.067
26.156
1.00
44.99


ATOM
1429
C
ARG
A
226
−14.180
54.585
24.825
1.00
46.52


ATOM
1430
O
ARG
A
226
−13.881
54.029
23.768
1.00
45.96


ATOM
1431
CB
ARG
A
226
−14.004
52.586
26.301
1.00
43.54


ATOM
1432
CG
ARG
A
226
−13.812
52.030
27.700
1.00
47.86


ATOM
1433
CD
ARG
A
226
−13.910
50.514
27.691
1.00
50.10


ATOM
1434
NE
ARG
A
225
−12.590
49.892
27.696
1.00
53.24


ATOM
1435
CZ
ARG
A
226
−12.229
48.890
26.904
1.00
61.97


ATOM
1436
NH1
ARG
A
226
−13.094
48.383
26.033
1.00
48.65


ATOM
1437
NH2
ARG
A
226
−11.007
48.388
26.989
1.00
45.92


ATOM
1438
N
SER
A
227
−14.981
55.642
24.886
1.00
41.79


ATOM
1439
CA
SER
A
227
−15.591
56.219
23.686
1.00
41.30


ATOM
1440
C
SER
A
227
−14.605
56.770
22.642
1.00
43.63


ATOM
1441
O
SER
A
227
−15.004
57.135
21.545
1.00
42.91


ATOM
1442
CB
SER
A
227
−16.634
57.277
24.060
1.00
44.89


ATOM
1443
OG
SER
A
227
−16.049
58.331
24.802
1.00
55.35


ATOM
1444
N
TYR
A
228
−13.320
56.808
22.975
1.00
40.05


ATOM
1445
CA
TYR
A
228
−12.310
57.302
22.027
1.00
39.45


ATOM
1446
C
TYR
A
228
−11.386
56.181
21.559
1.00
45.05


ATOM
1447
O
TYR
A
228
−10.394
56.425
20.862
1.00
45.05


ATOM
1448
CB
TYR
A
228
−11.502
58.452
22.640
1.00
39.38


ATOM
1449
CG
TYR
A
228
−12.324
59.703
22.877
1.00
39.22


ATOM
1450
CD1
TYR
A
228
−12.550
60.613
21.856
1.00
40.69


ATOM
1451
CD2
TYR
A
228
−12.911
59.948
24.111
1.00
39.22


ATOM
1452
CE1
TYR
A
228
−13.318
61.742
22.065
1.00
40.69


ATOM
1453
CE2
TYR
A
228
−13.677
61.075
24.329
1.00
39.41


ATOM
1454
CZ
TYR
A
228
−13.860
61.978
23.310
1.00
45.47


ATOM
1455
OH
TYR
A
228
−14.643
63.093
23.528
1.00
44.39


ATOM
1456
N
MET
A
229
−11.733
54.948
21.921
1.00
42.39


ATOM
1457
CA
MET
A
229
−10.937
53.783
21.554
1.00
42.47


ATOM
1458
C
MET
A
229
−11.210
53.319
20.139
1.00
45.87


ATOM
1459
O
MET
A
229
−12.352
53.332
19.678
1.00
45.68


ATOM
1460
CB
MET
A
229
−11.196
52.642
22.524
1.00
45.28


ATOM
1461
CG
MET
A
229
−10.745
52.927
23.935
1.00
49.39


ATOM
1462
SD
MET
A
229
−10.418
51.427
24.842
1.00
54.15


ATOM
1463
CE
MET
A
229
−10.636
52.009
26.504
1.00
50.79


ATOM
1464
N
SER
A
230
−10.159
52.877
19.461
1.00
42.43


ATOM
1465
CA
SER
A
230
−10.281
52.390
18.097
1.00
42.55


ATOM
1466
C
SER
A
230
−11.089
51.105
18.050
1.00
48.03


ATOM
1467
O
SER
A
230
−11.181
50.376
19.039
1.00
48.19


ATOM
1468
CB
SER
A
230
−8.903
52.153
17.492
1.00
45.98


ATOM
1469
OG
SER
A
230
−8.176
51.198
18.250
1.00
55.14


ATOM
1470
N
PRO
A
231
−11.664
50.825
16.887
1.00
45.06


ATOM
1471
CA
PRO
A
231
−12.446
49.616
16.690
1.00
44.36


ATOM
1472
C
PRO
A
231
−11.633
48.368
17.032
1.00
47.79


ATOM
1473
O
PRO
A
231
−12.150
47.434
17.633
1.00
47.41


ATOM
1474
CB
PRO
A
231
−12.745
49.644
15.187
1.00
45.76


ATOM
1475
CG
PRO
A
231
−12.708
51.056
14.825
1.00
50.03


ATOM
1476
CD
PRO
A
231
−11.663
51.681
15.688
1.00
45.46


ATOM
1477
N
GLU
A
232
−10.361
48.357
16.637
1.00
44.32


ATOM
1478
CA
GLU
A
232
−9.486
47.205
16.880
1.00
44.36


ATOM
1479
C
GLU
A
232
−9.165
46.966
18.358
1.00
50.32


ATOM
1480
O
GLU
A
232
−8.903
45.832
18.764
1.00
50.79


ATOM
1481
CB
GLU
A
232
−8.203
47.282
16.038
1.00
45.35


ATOM
1482
CG
GLU
A
232
−7.183
48.291
16.531
1.00
52.47


ATOM
1483
CD
GLU
A
232
−7.301
49.628
15.828
1.00
62.98


ATOM
1484
OE1
GLU
A
232
−8.362
49.896
15.222
1.00
43.15


ATOM
1485
OE2
GLU
A
232
−6.333
50.414
15.858
1.00
57.26


ATOM
1486
N
ARG
A
233
−9.214
43.021
19.160
1.00
47.31


ATOM
1487
CA
ARG
A
233
−8.967
47.893
20.590
1.00
47.31


ATOM
1488
C
ARG
A
233
−10.238
47.453
21.303
1.00
51.94


ATOM
1489
O
ARG
A
233
−10.193
46.764
22.208
1.00
51.42


ATOM
1490
CB
ARG
A
233
−8.448
49.204
21.178
1.00
46.85


ATOM
1491
CG
ARG
A
233
−6.929
49.283
21.220
1.00
53.10


ATOM
1492
CD
ARG
A
233
−6.454
50.438
22.070
1.00
55.67


ATOM
1493
NE
ARG
A
233
−6.358
50.083
23.483
1.00
58.30


ATOM
1494
CZ
ARG
A
233
−6.100
50.953
24.454
1.00
71.14


ATOM
1495
NH1
ARG
A
233
−5.898
52.239
24.160
1.00
54.30


ATOM
1496
NH2
ARG
A
233
−6.040
50.542
25.720
1.00
58.79


ATOM
1497
N
LEU
A
234
−11.382
47.848
20.764
1.00
49.90


ATOM
1498
CA
LEU
A
234
−12.667
47.474
21.343
1.00
50.33


ATOM
1499
C
LEU
A
234
−13.011
46.032
20.954
1.00
56.31


ATOM
1500
O
LEU
A
234
−13.972
45.449
21.462
1.00
54.93


ATOM
1501
CB
LEU
A
234
−13.768
48.409
20.830
1.00
50.27


ATOM
1502
CG
LEU
A
234
−13.753
49.866
21.285
1.00
54.72


ATOM
1503
CD1
LEU
A
234
−14.979
50.589
20.740
1.00
54.34


ATOM
1504
CD2
LEU
A
234
−13.702
49.953
22.808
1.00
57.30


ATOM
1505
N
GLN
A
235
−12.237
45.478
20.024
1.00
55.21


ATOM
1506
CA
GLN
A
235
−12.485
44.134
19.523
1.00
56.04


ATOM
1507
C
GLN
A
235
−11.496
43.123
20.070
1.00
63.39


ATOM
1508
O
GLN
A
235
−11.496
41.967
19.659
1.00
63.02


ATOM
1509
CB
GLN
A
235
−12.451
44.122
17.999
1.00
57.16


ATOM
1510
CG
GLN
A
235
−13.819
44.250
17.345
1.00
73.73


ATOM
1511
CD
GLN
A
235
−13.786
43.929
15.857
1.00
98.56


ATOM
1512
OE1
GLN
A
235
−12.715
43.827
15.254
1.00
94.22


ATOM
1513
NE2
GLN
A
235
−14.964
43.779
15.257
1.00
93.06


ATOM
1514
N
GLY
A
236
−10.651
43.564
20.995
1.00
62.67


ATOM
1515
CA
GLY
A
236
−9.666
42.690
21.605
1.00
63.77


ATOM
1516
C
GLY
A
236
−8.428
42.550
20.732
1.00
71.88


ATOM
1517
O
GLY
A
236
−7.346
42.219
21.226
1.00
72.01


ATOM
1518
N
THR
A
237
−8.582
42.793
19.434
1.00
71.24


ATOM
1519
CA
THR
A
237
−7.447
42.704
18.514
1.00
72.48


ATOM
1520
C
THR
A
237
−6.327
43.624
18.992
1.00
79.34


ATOM
1521
O
THR
A
237
−6.529
44.831
19.150
1.00
79.03


ATOM
1522
CB
THR
A
237
−7.837
43.100
17.092
1.00
80.43


ATOM
1523
OG1
THR
A
237
−8.461
41.985
16.442
1.00
80.39


ATOM
1524
CG2
THR
A
237
−6.604
43.517
16.308
1.00
78.79


ATOM
1525
N
HIS
A
238
−5.153
43.052
19.247
1.00
77.92


ATOM
1526
CA
HIS
A
238
−4.038
43.846
19.753
1.00
78.42


ATOM
1527
C
HIS
A
238
−3.758
45.120
18.960
1.00
80.72


ATOM
1528
O
HIS
A
238
−3.823
45.139
17.722
1.00
80.32


ATOM
1529
CB
HIS
A
238
−2.773
43.011
19.984
1.00
79.87


ATOM
1530
CG
HIS
A
238
−2.095
43.313
21.284
1.00
83.80


ATOM
1531
ND1
HIS
A
238
−2.778
43.364
22.482
1.00
85.91


ATOM
1532
CD2
HIS
A
238
−0.812
43.644
21.568
1.00
85.89


ATOM
1533
CE1
HIS
A
238
−1.938
43.683
23.452
1.00
85.44


ATOM
1534
NE2
HIS
A
238
−0.740
43.859
22.924
1.00
85.81


ATOM
1535
N
TYR
A
239
−3.482
46.192
19.697
1.00
75.51


ATOM
1536
CA
TYR
A
239
−2.295
47.510
19.122
1.00
74.27


ATOM
1537
C
TYR
A
239
−1.843
47.995
19.127
1.00
75.07


ATOM
1538
O
TYR
A
239
−0.963
47.405
19.763
1.00
74.49


ATOM
1539
CB
TYR
A
239
−4.128
48.513
19.892
1.00
75.47


ATOM
1540
CG
TYR
A
239
−3.829
48.518
21.378
1.00
77.30


ATOM
1541
CD1
TYR
A
239
−4.067
47.391
22.159
1.00
79.17


ATOM
1542
CD2
TYR
A
239
−3.287
49.639
21.996
1.00
77.98


ATOM
1543
CE1
TYR
A
239
−3.797
47.390
23.515
1.00
79.94


ATOM
1544
CE2
TYR
A
239
−3.017
49.650
23.354
1.00
78.79


ATOM
1545
CZ
TYR
A
239
−3.269
48.523
24.109
1.00
85.40


ATOM
1546
OH
TYR
A
239
−2.997
48.530
25.460
1.00
84.74


ATOM
1547
N
SER
A
240
−1.640
49.124
18.455
1.00
69.15


ATOM
1548
CA
SER
A
240
−0.354
49.788
18.387
1.00
67.52


ATOM
1549
C
SER
A
240
−0.623
51.287
18.403
1.00
67.85


ATOM
1550
O
SER
A
240
−1.729
51.717
18.724
1.00
67.55


ATOM
1551
CB
SER
A
240
0.372
49.406
17.101
1.00
71.07


ATOM
1552
OG
SER
A
240
−0.191
50.074
15.987
1.00
80.28


ATOM
1553
N
VAL
A
241
0.379
52.079
18.342
1.00
61.75


ATOM
1554
CA
VAL
A
241
0.223
53.531
18.001
1.00
59.90


ATOM
1555
C
VAL
A
241
−0.923
53.898
17.066
1.00
60.01


ATOM
1556
O
VAL
A
241
−1.472
54.997
17.134
1.00
59.20


ATOM
1557
CB
VAL
A
241
1.512
54.223
17.519
1.00
63.67


ATOM
1558
CG1
VAL
A
241
1.734
53.959
16.044
1.00
63.49


ATOM
1559
CG2
VAL
A
241
1.451
55.710
17.791
1.00
63.44


ATOM
1560
N
GLN
A
242
−1.287
52.958
16.202
1.00
54.26


ATOM
1561
CA
GLN
A
242
−2.367
53.165
15.250
1.00
53.01


ATOM
1562
C
GLN
A
242
−3.701
53.410
15.948
1.00
55.09


ATOM
1563
O
GLN
A
242
−4.621
53.977
15.361
1.00
54.90


ATOM
1564
CB
GLN
A
242
−2.478
51.976
14.303
1.00
54.09


ATOM
1565
CG
GLN
A
242
−1.290
51.824
13.371
1.00
62.48


ATOM
1566
CD
GLN
A
242
−1.221
52.924
12.331
1.00
78.14


ATOM
1567
OE1
GLN
A
242
−0.399
53.838
12.431
1.00
71.54


ATOM
1568
NE2
GLN
A
242
−2.078
52.835
11.315
1.00
71.78


ATOM
1569
N
SER
A
243
−3.803
52.985
17.203
1.00
49.60


ATOM
1570
CA
SER
A
243
−5.021
53.196
17.972
1.00
48.12


ATOM
1571
C
SER
A
243
−5.068
54.641
18.467
1.00
48.31


ATOM
1572
O
SER
A
243
−6.134
55.250
18.566
1.00
47.13


ATOM
1573
CB
SER
A
243
−5.082
52.230
19.146
1.00
51.93


ATOM
1574
CG
SER
A
243
−5.147
50.898
18.688
1.00
62.25


ATOM
1575
N
ASP
A
244
−3.896
55.187
18.747
1.00
42.87


ATOM
1576
CA
ASP
A
244
−3.781
56.558
19.213
1.00
41.70


ATOM
1577
C
ASP
A
244
−4.098
57.535
18.085
1.00
44.16


ATOM
1578
O
ASP
A
244
−4.654
58.603
18.320
1.00
44.23


ATOM
1579
CB
ASP
A
244
−2.385
56.811
19.783
1.00
42.93


ATOM
1580
CG
ASP
A
244
−2.160
56.093
21.098
1.00
48.67


ATOM
1581
CD1
ASP
A
244
−3.154
55.885
21.844
1.00
48.79


ATOM
1582
CD2
ASP
A
244
−1.004
55.711
21.374
1.00
51.75


ATOM
1583
N
ILE
A
245
−3.789
57.134
16.854
1.00
39.08


ATOM
1584
CA
ILE
A
245
−4.080
57.958
15.683
1.00
38.11


ATOM
1585
C
ILE
A
245
−5.594
58.024
15.462
1.00
41.38


ATOM
1586
O
ILE
A
245
−6.144
59.080
15.143
1.00
40.96


ATOM
1587
CB
ILE
A
245
−3.371
57.420
14.418
1.00
40.49


ATOM
1588
CG1
ILE
A
245
−1.869
57.768
14.458
1.00
40.07


ATOM
1589
CG2
ILE
A
245
−4.037
57.957
13.151
1.00
40.33


ATOM
1590
CD1
ILE
A
245
−1.088
57.237
13.284
1.00
41.82


ATOM
1591
N
TRP
A
246
−6.270
56.907
15.686
1.00
37.64


ATOM
1592
CA
TRP
A
246
−7.715
56.876
15.545
1.00
37.39


ATOM
1593
C
TRP
A
246
−8.324
57.854
16.536
1.00
41.57


ATOM
1594
O
TRP
A
246
−9.210
58.636
16.192
1.00
42.32


ATOM
1595
CB
TRP
A
246
−8.258
55.464
15.826
1.00
35.87


ATOM
1596
CG
TRP
A
246
−9.720
55.464
16.217
1.00
36.79


ATOM
1597
CD1
TRP
A
246
−10.252
55.767
17.454
1.00
39.55


ATOM
1598
CD2
TRP
A
246
−10.834
55.206
15.359
1.00
36.57


ATOM
1599
NE1
TRP
A
246
−11.625
55.691
17.410
1.00
38.75


ATOM
1600
CE2
TRP
A
246
−12.010
55.355
16.139
1.00
40.25


ATOM
1601
CE3
TRP
A
246
−10.957
54.822
14.021
1.00
37.90


ATOM
1602
CZ2
TRP
A
246
−13.285
55.144
15.616
1.00
39.78


ATOM
1603
CZ3
TRP
A
246
−12.234
54.622
13.497
1.00
39.41


ATOM
1604
CH2
TRP
A
246
−13.376
54.786
14.295
1.00
40.12


ATOM
1605
N
SER
A
247
−7.868
57.765
17.785
1.00
36.94


ATOM
1606
CA
SER
A
247
−8.368
58.602
18.871
1.00
35.64


ATOM
1607
C
SER
A
247
−8.131
60.071
18.567
1.00
39.21


ATOM
1608
O
SER
A
247
−8.981
60.920
18.855
1.00
38.67


ATOM
1609
CB
SER
A
247
−7.687
58.220
20.193
1.00
37.39


ATOM
1610
OG
SER
A
247
−7.855
56.841
20.466
1.00
41.56


ATOM
1611
N
MET
A
248
−6.972
60.375
17.983
1.00
34.98


ATOM
1612
CA
MET
A
248
−6.673
61.739
17.624
1.00
34.50


ATOM
1613
C
MET
A
248
−7.682
62.203
16.594
1.00
37.58


ATOM
1614
O
MET
A
248
−8.251
63.293
16.714
1.00
37.19


ATOM
1615
CB
MET
A
248
−5.261
61.870
17.071
1.00
36.91


ATOM
1616
CG
MET
A
248
−4.938
63.289
16.616
1.00
40.41


ATOM
1617
SD
MET
A
248
−3.378
63.426
15.807
1.00
44.67


ATOM
1618
CE
MET
A
248
−3.649
62.370
14.361
1.00
41.23


ATOM
1619
N
GLY
A
249
−7.929
61.353
15.595
1.00
33.38


ATOM
1620
CA
GLY
A
249
−8.895
61.651
14.534
1.00
33.05


ATOM
1621
C
GLY
A
249
−10.301
61.893
15.095
1.00
37.52


ATOM
1622
O
GLY
A
249
−10.998
62.833
14.685
1.00
37.85


ATOM
1623
N
LEU
A
250
−10.725
61.045
16.022
1.00
33.69


ATOM
1624
CA
LEU
A
250
−12.049
61.197
16.625
1.00
34.09


ATOM
1625
C
LEU
A
250
−12.158
62.506
17.446
1.00
37.41


ATOM
1626
O
LEU
A
250
−13.153
63.230
17.361
1.00
36.25


ATOM
1627
CB
LEU
A
250
−12.400
59.978
17.499
1.00
34.10


ATOM
1628
CG
LEU
A
250
−13.851
59.956
17.991
1.00
38.67


ATOM
1629
CD1
LEU
A
250
−14.806
59.844
16.819
1.00
38.90


ATOM
1630
CD2
LEU
A
250
−14.085
58.651
18.999
1.00
40.43


ATOM
1631
N
SER
A
251
−11.125
62.787
18.236
1.00
33.92


ATOM
1632
CA
SER
A
251
−11.075
64.001
19.047
1.00
33.46


ATOM
1633
C
SER
A
251
−11.093
65.257
18.159
1.00
37.66


ATOM
1634
O
SER
A
251
−11.734
66.257
18.490
1.00
37.13


ATOM
1635
CB
SER
A
251
−9.820
63.996
19.930
1.00
35.87


ATOM
1636
OG
SER
A
251
−9.746
62.813
20.707
1.00
41.13


ATOM
1637
N
LEU
A
252
−10.407
65.185
17.021
1.00
34.60


ATOM
1638
CA
LEU
A
252
−10.348
65.307
16.088
1.00
34.61


ATOM
1639
C
LEU
A
252
−11.713
66.646
15.497
1.00
38.65


ATOM
1640
O
LEU
A
252
−12.079
67.816
15.390
1.00
38.56


ATOM
1641
CB
LEU
A
252
−9.324
66.038
14.977
1.00
34.62


ATOM
1642
CG
LEU
A
252
−7.860
65.248
15.401
1.00
39.14


ATOM
1643
CD1
LEU
A
252
−6.877
65.790
14.324
1.00
38.67


ATOM
1644
CD2
LEU
A
252
−7.608
67.712
15.791
1.00
40.91


ATOM
1645
N
VAL
A
253
−12.461
65.622
15.106
1.00
35.10


ATOM
1646
CA
VAL
A
253
−13.790
65.824
14.536
1.00
34.41


ATOM
1647
C
VAL
A
253
−14.726
66.415
15.585
1.00
37.88


ATOM
1648
O
VAL
A
253
−15.511
67.330
15.303
1.00
36.86


ATOM
1649
CB
VAL
A
253
−14.391
64.503
14.007
1.00
38.11


ATOM
1650
CG1
VAL
A
253
−15.828
64.717
13.555
1.00
37.78


ATOM
1651
CG2
VAL
A
253
−13.537
63.941
12.869
1.00
37.79


ATOM
1652
N
GLU
A
254
−14.634
65.908
16.806
1.00
34.84


ATOM
1653
CA
GLU
A
254
−15.480
66.413
17.869
1.00
34.60


ATOM
1654
C
GLU
A
254
−15.242
67.893
18.083
1.00
39.49


ATOM
1655
O
GLU
A
254
−16.193
68.576
18.186
1.00
40.17


ATOM
1656
CB
GLU
A
254
−15.239
65.672
19.166
1.00
35.03


ATOM
1657
CG
GLU
A
254
−15.695
66.475
20.386
1.00
43.24


ATOM
1658
CD
GLU
A
254
−15.806
65.638
21.639
1.00
48.03


ATOM
1659
OE1
GLU
A
254
−15.134
54.591
21.736
1.00
38.84


ATOM
1660
OE2
GLU
A
254
−16.554
66.038
22.540
1.00
39.22


ATOM
1661
N
MET
A
255
−13.969
58.279
18.154
1.00
35.02


ATOM
1662
CA
MET
A
255
−13.596
59.673
18.394
1.00
34.71


ATOM
1663
C
MET
A
255
−13.960
70.518
17.258
1.00
39.19


ATOM
1664
O
MET
A
255
−14.327
71.765
17.497
1.00
39.09


ATOM
1665
CB
MET
A
255
−12.105
69.787
18.741
1.00
36.92


ATOM
1666
CG
MET
A
255
−11.715
69.056
20.013
1.00
40.35


ATOM
1667
SD
MET
A
255
−9.994
69.277
20.476
1.00
44.80


ATOM
1668
CE
MET
A
255
−9.180
68.154
19.349
1.00
41.04


ATOM
1669
N
ALA
A
255
−13.870
70.131
16.020
1.00
36.01


ATOM
1670
CA
ALA
A
256
−14.201
70.944
14.846
1.00
35.73


ATOM
1671
C
ALA
A
256
−15.708
71.136
14.689
1.00
40.24


ATOM
1672
O
ALA
A
256
−16.166
72.173
14.210
1.00
39.14


ATOM
1673
CB
ALA
A
256
−13.625
70.320
13.595
1.00
36.49


ATOM
1674
N
VAL
A
257
−16.477
70.116
15.053
1.00
37.86


ATOM
1675
CA
VAL
A
257
−17.917
70.200
14.924
1.00
37.90


ATOM
1676
C
VAL
A
257
−18.554
70.638
16.216
1.00
42.96


ATOM
1677
O
VAL
A
257
−19.721
71.086
16.207
1.00
42.29


ATOM
1678
CB
VAL
A
257
−18.534
68.899
14.354
1.00
41.41


ATOM
1679
CG1
VAL
A
257
−17.803
68.494
13.078
1.00
40.88


ATOM
1680
CG2
VAL
A
257
−18.492
67.771
15.386
1.00
41.29


ATOM
1681
N
GLY
A
258
−17.840
70.558
17.320
1.00
40.92


ATOM
1682
CA
GLY
A
258
−18.336
70.995
18.622
1.00
41.01


ATOM
1683
C
GLY
A
258
−19.228
69.963
19.316
1.00
45.42


ATOM
1684
O
GLY
A
258
−20.041
70.309
20.164
1.00
45.12


ATOM
1685
N
ARG
A
259
−19.045
68.696
18.989
1.00
42.55


ATOM
1686
CA
ARG
A
259
−19.850
67.647
19.607
1.00
43.04


ATOM
1687
C
ARG
A
259
−19.243
66.262
19.367
1.00
47.11


ATOM
1688
O
ARG
A
259
−18.663
66.008
18.308
1.00
47.22


ATOM
1689
CB
ARG
A
259
−21.277
67.698
19.047
1.00
44.79


ATOM
1690
CG
ARG
A
259
−22.087
66.445
19.270
1.00
55.86


ATOM
1691
CD
ARG
A
259
−23.063
66.210
18.128
1.00
67.50


ATOM
1692
NE
ARG
A
259
−22.583
65.175
17.219
1.00
76.61


ATOM
1693
CZ
ARG
A
259
−23.209
64.028
16.989
1.00
85.04


ATOM
1694
NH1
ARG
A
259
−24.361
63.766
17.586
1.00
68.22


ATOM
1695
NH2
ARG
A
259
−22.682
63.145
16.156
1.00
72.71


ATOM
1696
N
TYR
A
260
−19.347
65.384
20.363
1.00
42.99


ATOM
1697
CA
TYR
A
260
−18.855
64.029
20.205
1.00
42.99


ATOM
1698
C
TYR
A
260
−19.564
63.476
18.967
1.00
49.21


ATOM
1699
O
TYR
A
260
−20.785
63.347
18.956
1.00
49.14


ATOM
1700
CB
TYR
A
260
−19.169
63.182
21.442
1.00
43.12


ATOM
1701
CG
TYR
A
260
−18.707
61.745
21.309
1.00
42.91


ATOM
1702
CD1
TYR
A
260
−17.372
61.396
21.526
1.00
44.14


ATOM
1703
CD2
TYR
A
260
−19.586
60.751
20.896
1.00
42.76


ATOM
1704
CE1
TYR
A
260
−16.947
60.091
21.373
1.00
43.39


ATOM
1705
CE2
TYR
A
260
−19.167
59.452
20.737
1.00
42.93


ATOM
1706
CZ
TYR
A
260
−17.855
59.122
20.975
1.00
47.95


ATOM
1707
OH
TYR
A
260
−17.452
57.815
20.821
1.00
46.61


ATOM
1708
N
PRO
A
261
−18.787
63.248
17.906
1.00
47.53


ATOM
1709
CA
PRO
A
261
−19.294
62.875
16.576
1.00
47.54


ATOM
1710
C
PRO
A
261
−20.097
61.581
16.353
1.00
53.60


ATOM
1711
O
PRO
A
261
−20.493
61.295
15.217
1.00
53.58


ATOM
1712
CB
PRO
A
261
−18.024
62.856
15.720
1.00
48.86


ATOM
1713
CG
PRO
A
261
−16.943
62.493
16.667
1.00
52.82


ATOM
1714
CD
PRO
A
261
−17.317
63.129
17.988
1.00
48.16


ATOM
1715
N
ILE
A
262
−20.330
60.802
17.399
1.00
51.36


ATOM
1716
CA
ILE
A
262
−21.074
59.549
17.243
1.00
51.94


ATOM
1717
C
ILE
A
262
−22.296
59.487
18.151
1.00
58.19


ATOM
1718
O
ILE
A
262
−22.207
59.785
19.334
1.00
57.62


ATOM
1719
CB
ILE
A
262
−20.180
58.324
17.507
1.00
54.85


ATOM
1720
CG1
ILE
A
262
−18.923
58.389
16.643
1.00
54.86


ATOM
1721
CG2
ILE
A
262
−20.945
57.033
17.242
1.00
55.67


ATOM
1722
CD1
ILE
A
262
−17.780
57.577
17.181
1.00
59.51


ATOM
1723
N
PRO
A
263
−23.440
59.097
17.590
1.00
57.19


ATOM
1724
CA
PRO
A
263
−23.542
58.760
16.181
1.00
57.55


ATOM
1725
C
PRO
A
263
−23.563
60.033
15.365
1.00
63.72


ATOM
1726
O
PRO
A
263
−23.714
61.113
15.911
1.00
63.00


ATOM
1727
CB
PRO
A
263
−24.903
56.081
16.100
1.00
58.93


ATOM
1728
CG
PRO
A
263
−25.731
58.789
17.151
1.00
63.03


ATOM
1729
CD
PRO
A
263
−24.761
59.385
18.171
1.00
58.11


ATOM
1730
N
PRO
A
264
−23.428
59.898
14.052
1.00
63.33


ATOM
1731
CA
PRO
A
264
−23.399
61.049
13.156
1.00
64.04


ATOM
1732
C
PRO
A
264
−24.549
62.034
13.365
1.00
71.72


ATOM
1733
O
PRO
A
264
−25.639
61.659
13.805
1.00
70.66


ATOM
1734
CB
PRO
A
264
−23.484
60.412
11.760
1.00
65.21


ATOM
1735
CG
PRO
A
264
−23.232
58.928
11.958
1.00
69.05


ATOM
1736
CD
PRO
A
264
−22.907
58.692
13.399
1.00
64.22


ATOM
1737
N
PRO
A
265
−24.287
63.299
13.045
1.00
72.26


ATOM
1738
CA
PRO
A
265
−25.284
64.361
13.178
1.00
73.10


ATOM
1739
C
PRO
A
265
−26.159
64.429
11.937
1.00
80.87


ATOM
1740
O
PRO
A
265
−25.658
64.578
10.823
1.00
80.64


ATOM
1741
CB
PRO
A
265
−24.430
65.629
13.265
1.00
74.48


ATOM
1742
CG
PRO
A
255
−23.112
65.164
13.796
1.00
78.40


ATOM
1743
CD
PRO
A
265
−22.911
63.795
13.230
1.00
73.18


ATOM
1744
N
ASP
A
266
−27.468
64.325
12.132
1.00
80.23


ATOM
1745
CA
ASP
A
266
−28.409
64.386
11.019
1.00
81.38


ATOM
1746
C
ASP
A
266
−28.318
65.738
10.313
1.00
87.63


ATOM
1747
O
ASP
A
266
−27.832
66.715
10.886
1.00
87.25


ATOM
1748
CB
ASP
A
266
−29.834
64.140
11.514
1.00
83.52


ATOM
1749
CG
ASP
A
266
−29.967
62.833
12.276
1.00
96.05


ATOM
1750
OD1
ASP
A
266
−29.039
61.997
12.195
1.00
96.73


ATOM
1751
OD2
ASP
A
266
−31.004
62.640
12.950
1.00
102.85


ATOM
1752
N
ALA
A
267
−28.774
65.783
9.062
1.00
85.94


ATOM
1753
CA
ALA
A
267
−28.726
67.011
8.265
1.00
86.57


ATOM
1754
C
ALA
A
267
−29.275
68.222
9.021
1.00
92.25


ATOM
1755
O
ALA
A
267
−28.734
69.326
8.926
1.00
91.87


ATOM
1756
CB
ALA
A
267
−29.473
66.821
6.949
1.00
87.30


ATOM
1757
N
LYS
A
268
−30.353
68.009
9.767
1.00
89.96


ATOM
1758
CA
LYS
A
268
−30.978
69.082
10.526
1.00
90.28


ATOM
1759
C
LYS
A
268
−30.075
69.591
11.648
1.00
94.50


ATOM
1760
O
LYS
A
268
−30.044
70.789
11.936
1.00
94.28


ATOM
1761
CB
LYS
A
268
−32.329
68.628
11.083
1.00
93.13


ATOM
1762
CG
LYS
A
268
−33.459
68.636
10.054
1.00
108.19


ATOM
1763
CD
LYS
A
268
−34.040
70.034
9.881
1.00
118.55


ATOM
1764
CE
LYS
A
268
−34.103
70.433
8.414
1.00
128.99


ATOM
1765
NZ
LYS
A
268
−34.114
71.912
8.242
1.00
137.24


ATOM
1766
N
GLU
A
269
−29.334
68.681
12.273
1.00
90.99


ATOM
1767
CA
GLU
A
269
−28.420
69.052
13.352
1.00
90.68


ATOM
1768
C
GLU
A
269
−27.247
69.866
12.810
1.00
94.18


ATOM
1769
O
GLU
A
269
−26.716
70.739
13.500
1.00
93.68


ATOM
1770
CB
GLU
A
269
−27.903
67.806
14.071
1.00
92.05


ATOM
1771
CG
GLU
A
269
−28.783
66.580
13.899
1.00
102.91


ATOM
1772
CD
GLU
A
269
−28.376
65.443
14.815
1.00
123.46


ATOM
1773
OE1
GLU
A
269
−27.782
65.722
15.881
1.00
120.18


ATOM
1774
OE2
GLU
A
269
−28.639
64.272
14.468
1.00
115.08


ATOM
1775
N
LEU
A
270
−26.852
69.575
11.574
1.00
90.55


ATOM
1776
CA
LEU
A
270
−25.752
70.280
10.927
1.00
90.12


ATOM
1777
C
LEU
A
270
−26.206
71.665
10.501
1.00
93.85


ATOM
1778
O
LEU
A
270
−25.458
72.638
10.607
1.00
93.05


ATOM
1779
CB
LEU
A
270
−25.270
69.501
9.703
1.00
90.19


ATOM
1780
CG
LEU
A
270
−24.472
68.228
9.980
1.00
94.77


ATOM
1781
CD1
LEU
A
270
−24.606
67.253
8.822
1.00
94.94


ATOM
1782
CD2
LEU
A
270
−23.010
68.561
10.247
1.00
97.28


ATOM
1783
N
GLU
A
271
−27.440
71.742
10.013
1.00
90.66


ATOM
1784
CA
GLU
A
271
−28.014
72.999
9.555
1.00
90.52


ATOM
1785
C
GLU
A
271
−28.004
74.062
10.658
1.00
94.01


ATOM
1786
O
GLU
A
271
−27.795
75.250
10.391
1.00
93.62


ATOM
1787
CB
GLU
A
271
−29.435
72.777
9.029
1.00
91.90


ATOM
1788
CG
GLU
A
271
−30.158
74.043
8.611
1.00
102.63


ATOM
1789
CD
GLU
A
271
−31.615
74.052
9.033
1.00
122.03


ATOM
1790
OE1
GLU
A
271
−32.450
73.499
8.287
1.00
119.39


ATOM
1791
OE2
GLU
A
271
−31.923
74.595
10.117
1.00
112.81


ATOM
1792
N
LEU
A
272
−28.211
73.629
11.898
1.00
90.31


ATOM
1793
CA
LEU
A
272
−28.214
74.547
13.033
1.00
90.00


ATOM
1794
C
LEU
A
272
−26.808
74.722
13.602
1.00
93.37


ATOM
1795
O
LEU
A
272
−26.551
75.649
14.375
1.00
93.08


ATOM
1796
CB
LEU
A
272
−29.168
74.056
14.127
1.00
90.01


ATOM
1797
CG
LEU
A
272
−30.192
72.987
13.733
1.00
94.82


ATOM
1798
CD1
LEU
A
272
−30.476
72.052
14.908
1.00
94.90


ATOM
1799
CD2
LEU
A
272
−31.477
73.633
13.228
1.00
97.17


ATOM
1800
N
MET
A
273
−25.900
73.829
13.216
1.00
89.26


ATOM
1801
CA
MET
A
273
−24.524
73.882
13.698
1.00
88.59


ATOM
1802
C
MET
A
273
−23.697
74.903
12.927
1.00
91.98


ATOM
1803
O
MET
A
273
−23.058
75.773
13.522
1.00
91.58


ATOM
1804
CB
MET
A
273
−23.871
72.501
13.616
1.00
90.74


ATOM
1805
CG
MET
A
273
−24.284
71.559
14.733
1.00
94.14


ATOM
1806
SD
MET
A
273
−23.671
69.883
14.506
1.00
98.13


ATOM
1807
CE
MET
A
273
−22.608
69.725
15.922
1.00
94.70


ATOM
1808
N
PHE
A
274
−23.718
74.794
11.601
1.00
88.08


ATOM
1809
CA
PHE
A
274
−22.955
75.702
10.747
1.00
87.45


ATOM
1810
C
PHE
A
274
−23.858
76.526
9.842
1.00
90.64


ATOM
1811
O
PHE
A
274
−23.381
77.356
9.070
1.00
89.83


ATOM
1812
CB
PHE
A
274
−21.939
74.919
9.910
1.00
89.08


ATOM
1813
CG
PHE
A
274
−21.049
74.018
10.721
1.00
90.42


ATOM
1814
CD1
PHE
A
274
−21.522
72.813
11.214
1.00
93.31


ATOM
1815
CD2
PHE
A
274
−19.739
74.378
10.991
1.00
92.44


ATOM
1816
CE1
PHE
A
274
−20.707
71.987
11.964
1.00
94.10


ATOM
1817
CE2
PHE
A
274
−18.919
73.552
11.741
1.00
95.17


ATOM
1818
CZ
PHE
A
274
−19.402
72.354
12.221
1.00
93.20


ATOM
1819
N
PRO
A
306
−30.639
59.550
24.276
1.00
73.43


ATOM
1820
CA
PRO
A
306
−29.207
59.493
23.984
1.00
72.52


ATOM
1821
C
PRO
A
306
−28.682
58.060
24.069
1.00
74.80


ATOM
1822
O
PRO
A
306
−29.168
57.255
24.872
1.00
75.01


ATOM
1823
CB
PRO
A
306
−28.588
60.353
25.091
1.00
74.12


ATOM
1824
CG
PRO
A
306
−29.676
61.279
25.502
1.00
78.78


ATOM
1825
CD
PRO
A
306
−30.948
60.499
25.361
1.00
74.04


ATOM
1826
N
MET
A
307
−27.693
57.751
23.232
1.00
69.00


ATOM
1827
CA
MET
A
307
−27.097
56.419
23.179
1.00
67.46


ATOM
1828
C
MET
A
307
−26.323
56.068
24.448
1.00
68.89


ATOM
1829
O
MET
A
307
−25.616
56.906
25.010
1.00
67.67


ATOM
1830
CB
MET
A
307
−26.165
56.312
21.970
1.00
69.59


ATOM
1831
CG
MET
A
307
−26.362
55.064
21.136
1.00
73.03


ATOM
1832
SD
MET
A
307
−25.117
54.897
19.841
1.00
77.00


ATOM
1833
CE
MET
A
307
−26.128
54.973
18.385
1.00
73.64


ATOM
1834
N
ALA
A
308
−26.440
54.810
24.876
1.00
64.10


ATOM
1835
CA
ALA
A
308
−25.708
54.320
26.039
1.00
63.30


ATOM
1836
C
ALA
A
308
−24.341
53.810
25.586
1.00
65.47


ATOM
1837
O
ALA
A
308
−24.167
53.433
24.424
1.00
64.78


ATOM
1838
CB
ALA
A
308
−26.489
53.218
26.736
1.00
63.97


ATOM
1839
N
ILE
A
309
−23.374
53.815
26.505
1.00
60.87


ATOM
1840
CA
ILE
A
309
−21.996
53.398
26.212
1.00
60.11


ATOM
1841
C
ILE
A
309
−21.867
52.158
25.338
1.00
62.20


ATOM
1842
O
ILE
A
309
−21.270
52.211
24.269
1.00
62.41


ATOM
1843
CB
ILE
A
309
−21.168
53.186
27.496
1.00
63.23


ATOM
1844
CG1
ILE
A
309
−21.894
53.765
28.708
1.00
63.88


ATOM
1845
CG2
ILE
A
309
−19.787
53.799
27.338
1.00
63.47


ATOM
1846
CD1
ILE
A
309
−22.060
55.282
22.668
1.00
72.01


ATOM
1847
N
PHE
A
310
−22.394
51.034
25.812
1.00
56.64


ATOM
1848
CA
PHE
A
310
−22.308
49.784
25.065
1.00
55.43


ATOM
1849
C
PHE
A
310
−22.834
49.935
23.641
1.00
58.27


ATOM
1850
O
PHE
A
310
−22.231
49.431
22.692
1.00
57.81


ATOM
1851
CB
PHE
A
310
−23.025
48.651
25.801
1.00
57.02


ATOM
1852
CG
PHE
A
310
−24.352
49.057
26.399
1.00
58.15


ATOM
1853
CD1
PHE
A
310
−25.535
48.864
25.699
1.00
61.02


ATOM
1854
CD2
PHE
A
310
−24.410
49.606
27.670
1.00
60.26


ATOM
1855
CE1
PHE
A
310
−26.755
49.229
26.252
1.00
62.04


ATOM
1856
CE2
PHE
A
310
−25.629
49.973
28.229
1.00
63.06


ATOM
1857
CZ
PHE
A
310
−26.803
49.722
27.517
1.00
61.16


ATOM
1858
N
GLU
A
311
−23.960
50.636
23.497
1.00
54.06


ATOM
1859
CA
GLU
A
311
−24.559
50.873
22.187
1.00
53.37


ATOM
1860
C
GLU
A
311
−23.599
51.699
21.361
1.00
56.37


ATOM
1861
O
GLU
A
311
−23.377
51.437
20.174
1.00
56.14


ATOM
1862
CB
GLU
A
311
−25.883
51.624
22.332
1.00
54.74


ATOM
1863
CG
GLU
A
311
−26.784
51.098
23.432
1.00
65.19


ATOM
1864
CD
GLU
A
311
−28.130
51.795
23.465
1.00
84.58


ATOM
1865
OE1
GLU
A
311
−28.153
53.039
23.559
1.00
82.82


ATOM
1866
OE2
GLU
A
311
−29.165
51.097
23.405
1.00
77.20


ATOM
1867
N
LEU
A
312
−23.008
52.693
22.006
1.00
51.70


ATOM
1868
CA
LEU
A
312
−22.048
53.557
21.355
1.00
51.07


ATOM
1869
C
LEU
A
312
−20.847
52.751
20.870
1.00
54.28


ATOM
1870
O
LEU
A
312
−20.449
52.845
19.709
1.00
54.05


ATOM
1871
CB
LEU
A
312
−21.595
54.646
22.325
1.00
50.96


ATOM
1872
CG
LEU
A
312
−20.963
55.895
21.722
1.00
55.13


ATOM
1873
CD1
LEU
A
312
−20.724
56.916
22.804
1.00
54.87


ATOM
1874
CD2
LEU
A
312
−19.668
55.533
21.025
1.00
57.92


ATOM
1875
N
LEU
A
313
−20.274
51.956
21.767
1.00
50.39


ATOM
1876
CA
LEU
A
313
−19.105
51.147
21.434
1.00
49.85


ATOM
1877
C
LEU
A
313
−19.368
50.198
20.277
1.00
53.39


ATOM
1878
O
LEU
A
313
−18.551
50.082
19.367
1.00
52.79


ATOM
1879
CB
LEU
A
313
−18.602
50.392
22.659
1.00
49.65


ATOM
1880
CG
LEU
A
313
−18.115
51.306
23.790
1.00
53.75


ATOM
1881
CD1
LEU
A
313
−17.506
50.501
24.928
1.00
53.25


ATOM
1882
CD2
LEU
A
313
−17.123
52.341
23.252
1.00
55.51


ATOM
1883
N
ASP
A
314
−20.522
49.546
20.295
1.00
50.39


ATOM
1884
CA
ASP
A
314
−20.887
48.641
19.216
1.00
50.69


ATOM
1885
C
ASP
A
314
−20.941
49.426
17.900
1.00
54.34


ATOM
1886
O
ASP
A
314
−20.404
48.986
16.873
1.00
53.55


ATOM
1887
CB
ASP
A
314
−22.238
47.971
19.512
1.00
53.25


ATOM
1888
CG
ASP
A
314
−22.645
46.969
18.440
1.00
66.96


ATOM
1889
OD1
ASP
A
314
−22.020
45.891
18.355
1.00
68.20


ATOM
1890
OD2
ASP
A
314
−23.513
47.250
17.701
1.00
74.96


ATOM
1891
N
TYR
A
315
−21.539
50.617
17.952
1.00
51.03


ATOM
1892
CA
TYR
A
315
−21.620
51.487
16.785
1.00
50.95


ATOM
1893
C
TYR
A
315
−20.221
51.724
16.198
1.00
54.02


ATOM
1894
O
TYR
A
315
−20.022
51.576
14.990
1.00
53.77


ATOM
1895
CB
TYR
A
315
−22.267
52.830
17.149
1.00
52.64


ATOM
1896
CG
TYR
A
315
−22.634
53.668
15.944
1.00
55.01


ATOM
1897
CD1
TYR
A
315
−21.652
54.303
15.186
1.00
56.88


ATOM
1898
CD2
TYR
A
315
−23.961
53.793
15.538
1.00
56.33


ATOM
1899
CE1
TYR
A
315
−21.984
55.057
14.059
1.00
57.98


ATOM
1900
CE2
TYR
A
315
−24.308
54.545
14.416
1.00
57.50


ATOM
1901
CZ
TYR
A
315
−23.315
55.177
13.682
1.00
65.59


ATOM
1902
OH
TYR
A
315
−23.658
55.916
12.568
1.00
65.66


ATOM
1903
N
ILE
A
316
−19.287
52.091
17.062
1.00
49.49


ATOM
1904
CA
ILE
A
316
−17.912
52.340
16.642
1.00
48.94


ATOM
1905
C
ILE
A
316
−17.325
51.135
15.908
1.00
52.51


ATOM
1906
O
ILE
A
316
−16.712
51.277
14.850
1.00
52.27


ATOM
1907
CB
ILE
A
316
−16.997
52.666
17.852
1.00
52.20


ATOM
1908
CG1
ILE
A
316
−17.380
54.013
18.484
1.00
52.39


ATOM
1909
CG2
ILE
A
316
−15.520
52.640
17.437
1.00
52.81


ATOM
1910
CD1
ILE
A
316
−16.896
54.178
19.916
1.00
55.78


ATOM
1911
N
VAL
A
317
−17.493
49.953
16.485
1.00
48.68


ATOM
1912
CA
VAL
A
317
−16.943
48.737
15.894
1.00
48.05


ATOM
1913
C
VAL
A
317
−17.713
48.271
14.665
1.00
51.58


ATOM
1914
O
VAL
A
317
−17.143
47.641
13.771
1.00
51.25


ATOM
1915
CB
VAL
A
317
−16.915
47.580
16.906
1.00
51.62


ATOM
1916
CG1
VAL
A
317
−16.165
46.393
16.339
1.00
51.23


ATOM
1917
CG2
VAL
A
317
−16.314
48.029
18.215
1.00
51.43


ATOM
1918
N
ASN
A
318
−19.008
48.572
14.627
1.00
47.64


ATOM
1919
CA
ASN
A
318
−19.865
48.097
13.545
1.00
47.09


ATOM
1920
C
ASN
A
318
−20.209
49.060
12.414
1.00
50.25


ATOM
1921
O
ASN
A
318
−20.425
48.631
11.285
1.00
49.16


ATOM
1922
CB
ASN
A
318
−21.123
47.460
14.113
1.00
46.66


ATOM
1923
CG
ASN
A
318
−20.828
46.191
14.855
1.00
60.86


ATOM
1924
OD1
ASN
A
318
−20.081
45.340
14.369
1.00
49.77


ATOM
1925
ND2
ASN
A
318
−21.315
46.098
16.084
1.00
53.58


ATOM
1926
N
GLU
A
319
−20.298
50.350
12.719
1.00
46.79


ATOM
1927
CA
GLU
A
319
−20.645
51.341
11.707
1.00
46.19


ATOM
1928
C
GLU
A
319
−19.404
51.940
11.056
1.00
48.94


ATOM
1929
O
GLU
A
319
−18.280
51.635
11.446
1.00
48.03


ATOM
1930
CB
GLU
A
319
−21.511
52.447
12.312
1.00
47.56


ATOM
1931
CG
GLU
A
319
−22.970
52.073
12.466
1.00
56.32


ATOM
1932
CD
GLU
A
319
−23.449
51.143
11.372
1.00
76.49


ATOM
1933
OE1
GLU
A
319
−23.326
51.502
10.185
1.00
75.45


ATOM
1934
OE2
GLU
A
319
−23.947
50.048
11.698
1.00
70.91


ATOM
1935
N
PRO
A
320
−19.614
52.786
10.050
1.00
45.18


ATOM
1936
CA
PRO
A
320
−18.498
53.437
9.363
1.00
44.08


ATOM
1937
C
PRO
A
320
−18.044
54.655
10.158
1.00
45.40


ATOM
1938
O
PRO
A
320
−18.842
55.312
10.821
1.00
44.03


ATOM
1939
CB
PRO
A
320
−19.104
53.849
8.017
1.00
45.63


ATOM
1940
CG
PRO
A
320
−20.195
52.853
7.791
1.00
50.24


ATOM
1941
CD
PRO
A
320
−20.776
52.600
9.158
1.00
45.54


ATOM
1942
N
PRO
A
321
−16.747
54.919
10.120
1.00
41.90


ATOM
1943
CA
PRO
A
321
−16.163
56.011
10.881
1.00
41.63


ATOM
1944
C
PRO
A
321
−16.825
57.351
10.609
1.00
46.31


ATOM
1945
O
PRO
A
321
−17.334
57.597
9.512
1.00
46.07


ATOM
1946
CB
PRO
A
321
−14.713
56.026
10.402
1.00
43.06


ATOM
1947
CG
PRO
A
321
−14.776
55.489
9.028
1.00
46.91


ATOM
1948
CD
PRO
A
321
−15.870
54.477
9.021
1.00
42.19


ATOM
1949
N
PRO
A
322
−16.813
58.217
11.619
1.00
42.65


ATOM
1950
CA
PRO
A
322
−17.377
59.559
11.492
1.00
41.89


ATOM
1951
C
PRO
A
322
−16.570
60.341
10.470
1.00
44.24


ATOM
1952
O
PRO
A
322
−15.510
59.897
10.036
1.00
43.91


ATOM
1953
CB
PRO
A
322
−17.165
60.172
12.892
1.00
43.60


ATOM
1954
CG
PRO
A
322
−16.799
59.016
13.791
1.00
47.85


ATOM
1955
CD
PRO
A
322
−16.143
58.012
12.914
1.00
43.09


ATOM
1956
N
LYS
A
323
−17.060
61.516
10.105
1.00
39.92


ATOM
1957
CA
LYS
A
323
−16.363
62.363
9.151
1.00
39.46


ATOM
1958
C
LYS
A
323
−16.828
63.807
9.272
1.00
43.88


ATOM
1959
O
LYS
A
323
−17.967
64.076
9.668
1.00
43.64


ATOM
1960
CB
LYS
A
323
−16.574
61.853
7.717
1.00
41.71


ATOM
1961
CG
LYS
A
323
−17.879
62.286
7.086
1.00
54.72


ATOM
1962
CD
LYS
A
323
−18.430
61.196
6.184
1.00
65.68


ATOM
1963
CE
LYS
A
323
−19.730
61.624
5.526
1.00
72.89


ATOM
1964
NZ
LYS
A
323
−19.490
62.340
4.242
1.00
81.65


ATOM
1965
N
LEU
A
324
−15.948
64.741
8.933
1.00
40.16


ATOM
1966
CA
LEU
A
324
−16.307
66.145
8.995
1.00
39.86


ATOM
1967
C
LEU
A
324
−17.369
66.433
7.948
1.00
44.51


ATOM
1968
O
LEU
A
324
−17.430
65.767
6.923
1.00
44.20


ATOM
1969
CB
LEU
A
324
−15.082
67.026
8.734
1.00
39.56


ATOM
1970
CG
LEU
A
324
−13.986
67.028
9.796
1.00
43.31


ATOM
1971
CD1
LEU
A
324
−12.711
67.608
9.212
1.00
43.13


ATOM
1972
CD2
LEU
A
324
−14.429
67.812
11.031
1.00
44.36


ATOM
1973
N
PRO
A
325
−18.197
67.438
8.200
1.00
41.82


ATOM
1974
CA
PRO
A
325
−19.200
67.838
7.221
1.00
41.62


ATOM
1975
C
PRO
A
325
−18.491
68.507
6.043
1.00
45.88


ATOM
1976
O
PRO
A
325
−17.480
69.191
6.220
1.00
45.15


ATOM
1977
CB
PRO
A
325
−20.051
68.879
7.985
1.00
43.07


ATOM
1978
CG
PRO
A
325
−19.279
69.190
9.241
1.00
47.16


ATOM
1979
CD
PRO
A
325
−18.510
67.950
9.542
1.00
42.29


ATOM
1980
N
SER
A
326
−19.024
68.312
4.846
1.00
43.38


ATOM
1981
CA
SER
A
326
−18.440
68.911
3.654
1.00
43.87


ATOM
1982
C
SER
A
326
−18.881
70.349
3.503
1.00
48.67


ATOM
1983
O
SER
A
326
−19.936
70.743
4.002
1.00
48.35


ATOM
1984
CB
SER
A
326
−18.829
68.121
2.405
1.00
47.70


ATOM
1985
OG
SER
A
326
−19.585
66.980
2.746
1.00
57.87


ATOM
1986
N
GLY
A
327
−18.079
71.127
2.788
1.00
46.32


ATOM
1987
CA
GLY
A
327
−18.391
72.528
2.550
1.00
46.24


ATOM
1988
C
GLY
A
327
−17.727
73.429
3.582
1.00
50.33


ATOM
1989
O
GLY
A
327
−17.021
74.386
3.226
1.00
50.48


ATOM
1990
N
VAL
A
328
−17.939
73.112
4.859
1.00
45.26


ATOM
1991
CA
VAL
A
328
−17.400
73.918
5.952
1.00
44.41


ATOM
1992
C
VAL
A
328
−15.900
73.761
6.247
1.00
46.05


ATOM
1993
O
VAL
A
328
−15.285
74.654
6.830
1.00
46.82


ATOM
1994
CB
VAL
A
328
−18.225
73.746
7.256
1.00
48.57


ATOM
1995
CG1
VAL
A
328
−19.463
74.607
7.201
1.00
48.45


ATOM
1996
CG2
VAL
A
328
−18.609
72.290
7.468
1.00
48.49


ATOM
1997
N
PHE
A
329
−15.313
72.634
5.861
1.00
39.33


ATOM
1998
CA
PHE
A
329
−13.893
72.404
6.130
1.00
37.23


ATOM
1999
C
PHE
A
329
−13.095
72.160
4.860
1.00
39.17


ATOM
2000
O
PHE
A
329
−13.647
71.733
3.842
1.00
39.14


ATOM
2001
CB
PHE
A
329
−13.712
71.241
7.099
1.00
38.27


ATOM
2002
CG
PHE
A
329
−14.266
71.504
8.464
1.00
39.19


ATOM
2003
CD1
PHE
A
329
−13.563
72.284
9.377
1.00
40.73


ATOM
2004
CD2
PHE
A
329
−15.503
70.996
8.836
1.00
41.09


ATOM
2005
CE1
PHE
A
329
−14.074
72.533
10.630
1.00
40.64


ATOM
2006
CE2
PHE
A
329
−16.017
71.246
10.102
1.00
43.05


ATOM
2007
CZ
PHE
A
329
−15.300
72.025
10.991
1.00
40.33


ATOM
2008
N
SER
A
330
−11.794
72.441
4.913
1.00
32.90


ATOM
2009
CA
SER
A
330
−10.949
72.228
3.750
1.00
31.42


ATOM
2010
C
SER
A
330
−10.891
70.742
3.428
1.00
35.79


ATOM
2011
O
SER
A
330
−11.042
69.888
4.314
1.00
34.36


ATOM
2012
CB
SER
A
330
−9.538
72.803
3.963
1.00
32.00


ATOM
2013
OG
SER
A
330
−8.750
71.960
4.778
1.00
37.87


ATOM
2014
N
LEU
A
331
−10.723
70.435
2.147
1.00
33.56


ATOM
2015
CA
LEU
A
331
−10.647
69.062
1.703
1.00
32.81


ATOM
2016
C
LEU
A
331
−9.439
68.411
2.339
1.00
35.96


ATOM
2017
O
LEU
A
331
−9.495
67.259
2.755
1.00
36.84


ATOM
2018
CB
LEU
A
331
−10.564
68.997
0.176
1.00
32.83


ATOM
2019
CG
LEU
A
331
−11.908
69.078
−0.562
1.00
38.09


ATOM
2020
CD1
LEU
A
331
−11.728
68.907
−2.068
1.00
38.59


ATOM
2021
CD2
LEU
A
331
−12.870
68.027
−0.023
1.00
41.23


ATOM
2022
N
GLU
A
332
−8.356
69.169
2.457
1.00
30.96


ATOM
2023
CA
GLU
A
332
−7.124
68.653
3.065
1.00
30.65


ATOM
2024
C
GLU
A
332
−7.368
68.196
4.490
1.00
35.13


ATOM
2025
O
GLU
A
332
−6.867
67.157
4.906
1.00
35.47


ATOM
2026
CB
GLU
A
332
−6.022
69.711
3.043
1.00
31.87


ATOM
2027
CG
GLU
A
332
−5.218
69.746
1.758
1.00
38.65


ATOM
2028
CD
GLU
A
332
−4.454
71.034
1.589
1.00
57.75


ATOM
2029
OE1
GLU
A
332
−4.615
71.934
2.433
1.00
57.70


ATOM
2030
OE2
GLU
A
332
−3.685
71.148
0.616
1.00
53.72


ATOM
2031
N
PHE
A
333
−8.130
68.990
5.238
1.00
31.46


ATOM
2032
CA
PHE
A
333
−8.469
68.665
6.622
1.00
30.98


ATOM
2033
C
PHE
A
333
−9.341
67.398
6.672
1.00
36.08


ATOM
2034
O
PHE
A
333
−9.076
66.476
7.459
1.00
36.58


ATOM
2035
CE
PHE
A
333
−9.190
69.851
7.284
1.00
32.36


ATOM
2036
CG
PHE
A
333
−9.440
69.673
8.761
1.00
33.55


ATOM
2037
CD1
PHE
A
333
−8.559
68.933
9.552
1.00
35.94


ATOM
2038
CD2
PHE
A
333
−10.559
70.245
9.365
1.00
35.10


ATOM
2039
OE1
PHE
A
333
−8.787
68.777
10.917
1.00
35.47


ATOM
2040
CE2
PHE
A
333
−10.794
70.089
10.737
1.00
37.67


ATOM
2041
CS
PHE
A
333
−9.914
69.360
11.510
1.00
35.69


ATOM
2042
N
GLN
A
334
−10.360
67.346
5.814
1.00
32.72


ATOM
2043
CA
GLN
A
334
−11.245
66.178
5.747
1.00
32.61


ATOM
2044
C
GLN
A
334
−10.437
64.927
5.385
1.00
38.01


ATOM
2045
O
GLN
A
334
−10.593
63.862
6.001
1.00
38.40


ATOM
2046
CB
GLN
A
334
−12.342
66.391
4.705
1.00
33.53


ATOM
2047
CG
GLN
A
334
−13.110
67.672
4.852
1.00
38.40


ATOM
2048
CD
GLN
A
334
−14.180
67.815
3.799
1.00
48.70


ATOM
2049
OE1
GLN
A
334
−14.779
66.839
3.387
1.00
44.73


ATOM
2050
NE2
GLN
A
334
−14.401
69.032
3.339
1.00
39.07


ATOM
2051
N
ASP
A
335
−9.573
65.051
4.392
1.00
33.66


ATOM
2052
CA
ASP
A
335
−8.765
63.925
4.011
1.00
33.57


ATOM
2053
C
ASP
A
335
−7.936
63.459
5.197
1.00
36.47


ATOM
2054
O
ASP
A
335
−7.860
62.257
5.478
1.00
36.86


ATOM
2055
CB
ASP
A
335
−7.860
64.256
2.821
1.00
35.18


ATOM
2056
CO
ASP
A
335
−7.080
63.034
2.323
1.00
39.38


ATOM
2057
OD1
ASP
A
335
−7.712
62.109
1.777
1.00
39.01


ATOM
2058
OD2
ASP
A
335
−5.850
62.985
2.525
1.00
43.27


ATOM
2059
N
PHE
A
336
−7.325
64.415
5.899
1.00
31.38


ATOM
2060
CA
PHE
A
336
−6.481
64.104
7.062
1.00
30.62


ATOM
2061
C
PHE
A
336
−7.231
63.299
8.136
1.00
35.05


ATOM
2062
O
PHE
A
336
−6.783
62.232
8.534
1.00
34.72


ATOM
2063
CB
PHE
A
336
−5.872
65.382
7.659
1.00
31.75


ATOM
2064
CG
PHE
A
336
−4.978
65.135
8.856
1.00
32.14


ATOM
2065
CD1
PHE
A
336
−3.634
64.825
8.686
1.00
34.30


ATOM
2066
CD2
PHE
A
336
−5.478
65.227
10.142
1.00
33.29


ATOM
2067
CE1
PHE
A
336
−2.803
64.602
9.790
1.00
34.74


ATOM
2068
CE2
PHE
A
336
−4.657
64.997
11.247
1.00
35.71


ATOM
2069
CZ
PHE
A
336
−3.314
64.682
11.062
1.00
33.62


ATOM
2070
N
VAL
A
337
−8.378
63.802
8.595
1.00
32.05


ATOM
2071
CA
VAL
A
337
−9.151
63.063
9.599
1.00
32.40


ATOM
2072
C
VAL
A
337
−9.518
61.719
9.035
1.00
37.60


ATOM
2073
O
VAL
A
337
−9.641
60.719
9.748
1.00
37.18


ATOM
2074
CB
VAL
A
337
−10.383
63.866
10.141
1.00
36.05


ATOM
2075
CG1
VAL
A
337
−9.932
65.158
10.840
1.00
35.81


ATOM
2076
CG2
VAL
A
337
−11.353
64.156
9.046
1.00
35.72


ATOM
2077
N
ASN
A
338
−9.978
61.701
7.747
1.00
34.40


ATOM
2078
CA
ASN
A
338
−10.427
60.469
7.084
1.00
33.83


ATOM
2079
C
ASN
A
338
−9.351
59.373
7.167
1.00
39.23


ATOM
2080
O
ASN
A
338
−9.656
58.211
7.440
1.00
39.14


ATOM
2081
CB
ASN
A
338
−10.772
60.737
5.616
1.00
27.49


ATOM
2082
CG
ASN
A
336
−12.217
61.208
5.414
1.00
37.50


ATOM
2083
OD1
ASN
A
338
−12.979
61.354
6.364
1.00
37.07


ATOM
2084
ND2
ASN
A
338
−12.572
61.479
4.179
1.00
27.35


ATOM
2085
N
LYS
A
339
−8.096
89.751
6.920
1.00
35.69


ATOM
2086
CA
LYS
A
339
−6.986
58.801
6.955
1.00
35.12


ATOM
2087
C
LYS
A
339
−6.657
58.350
8.386
1.00
40.03


ATOM
2088
O
LYS
A
339
−5.976
57.335
8.588
1.00
39.57


ATOM
2089
CB
LYS
A
339
−5.747
59.404
6.290
1.00
36.70


ATOM
2090
CG
LYS
A
339
−5.774
59.406
4.757
1.00
31.89


ATOM
2091
CD
LYS
A
339
−4.549
60.118
4.214
1.00
36.91


ATOM
2092
CE
LYS
A
339
−4.292
59.782
2.753
1.00
39.46


ATOM
2093
NZ
LYS
A
339
−5.532
59.863
1.929
1.00
39.18


ATOM
2094
N
CYS
A
340
−7.138
59.106
9.372
1.00
37.24


ATOM
2095
CA
CYS
A
340
−5.918
58.776
10.787
1.00
37.06


ATOM
2096
C
CYS
A
340
−8.011
57.815
11.258
1.00
41.14


ATOM
2097
O
CYS
A
340
−7.777
56.961
12.114
1.00
39.95


ATOM
2098
CB
CYS
A
340
−6.996
60.045
11.654
1.00
37.27


ATOM
2099
SG
CYS
A
340
−5.507
61.086
11.700
1.00
41.23


ATOM
2100
N
LEU
A
341
−9.215
58.000
10.713
1.00
38.31


ATOM
2101
CA
LEU
A
341
−10.389
57.241
11.123
1.00
38.32


ATOM
2102
C
LEU
A
341
−10.701
55.998
10.277
1.00
44.58


ATOM
2103
O
LEU
A
341
−11.820
55.472
10.319
1.00
44.15


ATOM
2104
CB
LEU
A
341
−11.605
58.169
11.202
1.00
37.79


ATOM
2105
CG
LEU
A
341
−11.457
59.276
12.254
1.00
41.32


ATOM
2106
CD1
LEU
A
341
−12.616
50.263
12.197
1.00
40.99


ATOM
2107
CD2
LEU
A
341
−11.329
58.675
13.640
1.00
41.77


ATOM
2108
N
ILE
A
342
−9.705
55.518
9.540
1.00
42.72


ATOM
2109
CA
ILE
A
342
−9.858
54.311
8.742
1.00
43.06


ATOM
2110
C
ILE
A
342
−9.872
53.105
9.695
1.00
48.09


ATOM
2111
O
ILE
A
342
−8.873
52.823
10.371
1.00
47.79


ATOM
2112
CB
ILE
A
342
−8.699
54.151
7.747
1.00
46.44


ATOM
2113
CG1
ILE
A
342
−8.926
55.054
6.524
1.00
46.60


ATOM
2114
CG2
ILE
A
342
−8.528
52.701
7.342
1.00
47.84


ATOM
2115
CD1
ILE
A
342
−7.686
55.294
5.700
1.00
48.39


ATOM
2116
N
LYS
A
343
−11.020
52.428
9.775
1.00
44.92


ATOM
2117
CA
LYS
A
343
−11.205
51.282
10.682
1.00
44.71


ATOM
2118
C
LYS
A
343
−10.092
50.221
10.670
1.00
48.96


ATOM
2119
O
LYS
A
343
−9.673
49.747
11.725
1.00
48.62


ATOM
2120
CB
LYS
A
343
−12.572
50.642
10.476
1.00
46.72


ATOM
2121
CG
LYS
A
343
−13.704
51.652
10.333
1.00
53.84


ATOM
2122
CD
LYS
A
343
−14.804
51.396
11.349
1.00
58.54


ATOM
2123
CE
LYS
A
343
−15.841
50.433
10.805
1.00
61.04


ATOM
2124
NZ
LYS
A
343
−16.530
49.698
11.887
1.00
64.56


ATOM
2125
N
ASN
A
344
−9.626
49.842
9.486
1.00
45.55


ATOM
2126
CA
ASN
A
344
−8.555
48.862
9.394
1.00
45.53


ATOM
2127
C
ASN
A
344
−7.229
49.527
9.762
1.00
50.33


ATOM
2128
O
ASN
A
344
−6.690
50.331
8.996
1.00
50.26


ATOM
2129
CB
ASN
A
344
−8.497
48.238
7.990
1.00
44.97


ATOM
2130
CG
ASN
A
344
−7.298
47.294
7.807
1.00
66.54


ATOM
2131
OD1
ASN
A
344
−6.548
47.022
8.753
1.00
58.45


ATOM
2132
ND2
ASN
A
344
−7.107
46.818
6.581
1.00
57.44


ATOM
2133
N
PRO
A
345
−6.719
49.199
10.944
1.00
47.24


ATOM
2134
CA
PRO
A
345
−5.475
49.789
11.436
1.00
46.96


ATOM
2135
C
PRO
A
345
−4.350
49.626
10.432
1.00
52.66


ATOM
2136
O
PRO
A
345
−3.362
50.374
10.457
1.00
52.02


ATOM
2137
CB
PRO
A
345
−5.174
48.981
12.719
1.00
48.28


ATOM
2138
CG
PRO
A
345
−5.998
47.746
12.612
1.00
52.10


ATOM
2139
CD
PRO
A
345
−7.214
48.128
11.830
1.00
47.63


ATOM
2140
N
ALA
A
346
−4.495
48.642
9.553
1.00
50.57


ATOM
2141
CA
ALA
A
346
−3.479
48.377
8.543
1.00
50.78


ATOM
2142
C
ALA
A
346
−3.504
49.471
7.479
1.00
54.61


ATOM
2143
O
ALA
A
346
−2.459
50.005
7.095
1.00
54.04


ATOM
2144
CB
ALA
A
346
−3.700
47.003
7.913
1.00
51.65


ATOM
2145
N
GLU
A
347
−4.708
49.811
7.026
1.00
51.28


ATOM
2146
CA
GLU
A
347
−4.890
50.853
6.020
1.00
51.00


ATOM
2147
C
GLU
A
347
−4.729
52.246
6.632
1.00
53.52


ATOM
2148
O
GLU
A
347
−4.268
53.171
5.969
1.00
57.83


ATOM
2149
CB
GLU
A
347
−6.271
50.734
5.381
1.00
52.60


ATOM
2150
CG
GLU
A
347
−6.477
49.463
4.590
1.00
66.92


ATOM
2151
CD
GLU
A
347
−7.936
49.216
4.271
1.00
97.76


ATOM
2152
OE1
GLU
A
347
−8.595
48.474
5.031
1.00
97.92


ATOM
2153
OE2
GLU
A
347
−8.435
49.724
3.273
1.00
97.70


ATOM
2154
N
ARG
A
348
−5.133
52.379
7.897
1.00
48.83


ATOM
2155
CA
ARG
A
348
−5.054
53.645
8.612
1.00
47.31


ATOM
2156
C
ARG
A
348
−3.667
54.243
8.481
1.00
49.67


ATOM
2157
O
ARG
A
348
−2.678
53.519
8.445
1.00
49.45


ATOM
2158
CB
ARG
A
348
−5.412
53.445
10.086
1.00
45.18


ATOM
2159
CG
ARG
A
348
−5.266
54.697
10.944
1.00
47.88


ATOM
2160
CD
ARG
A
348
−6.042
54.571
12.241
1.00
45.61


ATOM
2161
NE
ARG
A
348
−7.086
53.549
12.157
1.00
46.91


ATOM
2162
CZ
ARG
A
348
−7.330
52.645
13.102
1.00
55.15


ATOM
2163
NH1
ARG
A
348
−6.614
52.630
14.211
1.00
40.79


ATOM
2164
NH2
ARG
A
348
−8.295
51.758
12.941
1.00
41.64


ATOM
2165
N
ALA
A
349
−3.599
55.570
8.400
1.00
44.69


ATOM
2166
CA
ALA
A
349
−2.324
56.263
8.257
1.00
43.85


ATOM
2167
C
ALA
A
349
−1.479
56.129
9.503
1.00
45.93


ATOM
2168
O
ALA
A
349
−2.001
55.999
10.604
1.00
46.35


ATOM
2169
CB
ALA
A
349
−2.550
57.741
7.929
1.00
44.44


ATOM
2170
N
ASP
A
350
−0.166
56.198
9.331
1.00
43.62


ATOM
2171
CA
ASP
A
350
0.743
56.113
10.456
1.00
43.17


ATOM
2172
C
ASP
A
350
1.403
57.462
10.739
1.00
46.08


ATOM
2173
O
ASP
A
350
1.293
58.398
9.942
1.00
45.76


ATOM
2174
CB
ASP
A
350
1.781
54.992
10.260
1.00
45.05


ATOM
2175
CG
ASP
A
350
2.700
55.231
9.065
1.00
56.68


ATOM
2176
OD1
ASP
A
350
3.080
56.394
8.805
1.00
57.50


ATOM
2177
OD2
ASP
A
350
3.109
54.234
8.434
1.00
63.60


ATOM
2178
N
LEU
A
351
2.075
57.557
11.878
1.00
41.50


ATOM
2179
CA
LEU
A
351
2.705
58.794
12.284
1.00
41.44


ATOM
2180
C
LEU
A
351
3.590
59.414
11.205
1.00
45.71


ATOM
2181
O
LEU
A
351
3.546
60.618
10.976
1.00
46.12


ATOM
2182
CB
LEU
A
351
3.494
58.599
13.593
1.00
41.46


ATOM
2183
CG
LEU
A
351
2.683
58.295
14.860
1.00
45.72


ATOM
2184
CD1
LEU
A
351
3.589
57.846
15.988
1.00
45.86


ATOM
2185
CD2
LEU
A
351
1.837
59.488
15.289
1.00
47.17


ATOM
2186
N
LYS
A
352
4.409
58.598
10.562
1.00
42.41


ATOM
2187
CA
LYS
A
352
5.326
59.102
9.540
1.00
42.43


ATOM
2188
C
LYS
A
352
4.584
59.662
8.333
1.00
46.73


ATOM
2189
O
LYS
A
352
4.999
60.653
7.749
1.00
46.71


ATOM
2190
CB
LYS
A
352
6.313
58.013
9.112
1.00
44.97


ATOM
2191
CG
LYS
A
352
6.858
58.193
7.703
1.00
62.12


ATOM
2192
CD
LYS
A
352
8.226
57.530
7.534
1.00
70.56


ATOM
2193
CE
LYS
A
352
9.252
58.512
6.981
1.00
78.34


ATOM
2194
NZ
LYS
A
352
10.473
57.822
6.473
1.00
86.81


ATOM
2195
N
GLN
A
353
3.477
59.023
7.972
1.00
43.24


ATOM
2196
CA
GLN
A
353
2.668
59.462
6.833
1.00
42.58


ATOM
2197
C
GLN
A
353
1.884
60.709
7.197
1.00
45.79


ATOM
2198
O
GLN
A
353
1.656
61.586
6.355
1.00
45.48


ATOM
2199
CB
GLN
A
353
1.702
58.352
6.407
1.00
43.97


ATOM
2200
CG
GLN
A
353
2.365
56.994
6.173
1.00
58.19


ATOM
2201
CD
GLN
A
353
1.360
55.884
5.878
1.00
77.84


ATOM
2202
OE1
GLN
A
353
0.498
55.569
6.702
1.00
74.20


ATOM
2203
NE2
GLN
A
353
1.497
55.260
4.717
1.00
68.99


ATOM
2204
N
LEU
A
354
1.472
60.791
8.460
1.00
41.38


ATOM
2205
CA
LEU
A
354
0.715
61.937
8.938
1.00
40.41


ATOM
2206
C
LEU
A
354
1.603
63.171
9.023
1.00
44.07


ATOM
2207
O
LEU
A
354
1.195
64.261
8.532
1.00
43.23


ATOM
2208
CB
LEU
A
354
0.062
61.629
10.285
1.00
40.10


ATOM
2239
CG
LEU
A
354
−1.134
60.672
10.178
1.00
43.76


ATOM
2210
CD1
LEU
A
354
−1.681
50.316
11.538
1.00
43.39


ATOM
2211
CD2
LEU
A
354
−2.217
61.251
9.287
1.00
44.97


ATOM
2212
N
MET
A
355
2.838
62.963
9.474
1.00
40.96


ATOM
2213
CA
MET
A
355
3.785
64.087
9.585
1.00
41.29


ATOM
2214
C
MET
A
355
3.965
64.853
8.270
1.00
45.21


ATOM
2215
O
MET
A
355
4.222
45.067
8.278
1.00
44.54


ATOM
2216
CB
MET
A
355
5.136
63.598
10.112
1.00
44.03


ATOM
2217
CG
MET
A
355
5.315
63.771
11.643
1.00
48.31


ATOM
2218
SD
MET
A
355
5.172
65.521
12.196
1.00
52.98


ATOM
2219
CE
MET
A
355
3.417
65.692
12.313
1.00
49.82


ATOM
2220
N
VAL
A
355
3.816
64.148
7.143
1.00
41.28


ATOM
2221
CA
VAL
A
356
3.962
64.772
5.830
1.00
40.34


ATOM
2222
C
VAL
A
356
2.672
64.871
5.046
1.00
43.06


ATOM
2223
O
VAL
A
356
2.690
65.009
3.821
1.00
43.16


ATOM
2224
CB
VAL
A
356
5.028
64.083
4.972
1.00
44.24


ATOM
2225
CG1
VAL
A
356
6.416
64.301
5.577
1.00
44.10


ATOM
2226
CG2
VAL
A
356
4.713
62.595
4.807
1.00
43.85


ATOM
2227
N
HIS
A
357
1.546
64.814
5.742
1.00
38.27


ATOM
2228
CA
HIS
A
357
0.254
64.959
5.086
1.00
36.78


ATOM
2229
C
HIS
A
357
0.062
66.440
4.730
1.00
40.05


ATOM
2230
O
HIS
A
357
0.464
67.325
5.488
1.00
40.00


ATOM
2231
CB
HIS
A
357
−0.875
64.482
6.016
1.00
37.03


ATOM
2232
CG
HIS
A
357
−2.225
64.447
5.368
1.00
40.43


ATOM
2233
ND1
HIS
A
357
−2.985
65.581
5.161
1.00
42.30


ATOM
2234
CD2
HIS
A
357
−2.962
63.410
4.902
1.00
41.86


ATOM
2235
CE1
HIS
A
357
−4.129
65.243
4.594
1.00
41.52


ATOM
2236
NE2
HIS
A
357
−4.141
63.932
4.424
1.00
41.76


ATOM
2237
N
ALA
A
358
−0.529
66.694
3.564
1.00
35.48


ATOM
2238
CA
ALA
A
358
−0.790
68.045
3.075
1.00
34.01


ATOM
2239
C
ALA
A
358
−1.357
68.963
4.151
1.00
39.22


ATOM
2240
O
ALA
A
358
−1.011
70.147
4.207
1.00
40.32


ATOM
2241
CB
ALA
A
358
−1.730
67.997
1.908
1.00
34.16


ATOM
2242
N
PHE
A
359
−2.283
68.443
4.960
1.00
34.57


ATOM
2243
CA
PHE
A
359
−2.912
69.255
5.999
1.00
33.38


ATOM
2244
C
PHE
A
359
−1.881
69.720
7.023
1.00
38.30


ATOM
2245
O
PHE
A
359
−1.927
70.848
7.500
1.00
36.99


ATOM
2246
CB
PHE
A
359
−4.061
68.501
6.677
1.00
33.99


ATOM
2247
CG
PHE
A
359
−4.621
69.193
7.897
1.00
34.00


ATOM
2248
CD1
PHE
A
359
−5.301
70.394
7.771
1.00
35.67


ATOM
2249
CD2
PHE
A
359
−4.478
68.622
9.154
1.00
34.37


ATOM
2250
CE1
PHE
A
359
−5.814
71.041
8.904
1.00
35.60


ATOM
2251
CE2
PHE
A
359
−4.983
69.265
10.273
1.00
36.33


ATOM
2252
CZ
PHE
A
359
−5.655
70.474
10.150
1.00
34.19


ATOM
2253
N
ILE
A
360
−0.964
68.824
7.365
1.00
36.54


ATOM
2254
CA
ILE
A
360
0.063
69.105
8.352
1.00
36.94


ATOM
2255
C
ILE
A
360
1.107
70.041
7.778
1.00
42.20


ATOM
2256
O
ILE
A
360
1.497
71.024
8.409
1.00
41.97


ATOM
2257
CB
ILE
A
360
0.729
67.797
8.839
1.00
39.83


ATOM
2258
CG1
ILE
A
350
−0.275
66.959
9.637
1.00
39.95


ATOM
2259
CG2
ILE
A
360
1.966
68.097
9.684
1.00
40.38


ATOM
2260
CD1
ILE
A
360
−0.859
67.676
10.845
1.00
41.38


ATOM
2261
N
LYS
A
361
1.536
69.745
5.563
1.00
39.80


ATOM
2262
CA
LYS
A
361
2.501
70.569
5.876
1.00
39.61


ATOM
2263
C
LYS
A
361
1.952
71.983
5.743
1.00
43.38


ATOM
2264
O
LYS
A
351
2.642
72.954
6.042
1.00
43.36


ATOM
2265
CB
LYS
A
361
2.814
69.978
4.502
1.00
41.98


ATOM
2266
CG
LYS
A
361
4.018
69.054
4.494
1.00
55.37


ATOM
2267
CD
LYS
A
361
3.770
67.824
3.624
1.00
69.40


ATOM
2268
CE
LYS
A
361
3.866
68.149
2.137
1.00
76.80


ATOM
2269
NZ
LYS
A
361
3.056
67.202
1.310
1.00
85.51


ATOM
2270
N
ARG
A
362
0.697
72.090
5.323
1.00
39.61


ATOM
2271
CA
ARG
A
362
0.053
73.390
5.169
1.00
39.29


ATOM
2272
C
ARG
A
362
−0.102
74.105
6.521
1.00
44.74


ATOM
2273
O
ARG
A
362
0.039
75.325
6.605
1.00
45.17


ATOM
2274
CB
ARG
A
362
−1.307
73.239
4.488
1.00
37.40


ATOM
2275
CG
ARG
A
362
−2.085
74.564
4.344
1.00
43.09


ATOM
2276
CD
ARG
A
362
−3.596
74.327
4.146
1.00
43.39


ATOM
2277
NE
ARG
A
362
−4.344
74.396
5.413
1.00
39.98


ATOM
2278
CZ
ARG
A
362
−5.568
73.500
5.592
1.00
45.67


ATOM
2279
NH1
ARG
A
362
−6.192
73.293
4.590
1.00
33.42


ATOM
2280
NH2
ARG
A
362
−6.175
74.019
6.772
1.00
25.08


ATOM
2281
N
SER
A
363
−0.373
73.336
7.572
1.00
41.12


ATOM
2282
CA
SER
A
363
−0.549
73.888
8.909
1.00
41.02


ATOM
2283
C
SER
A
363
0.774
74.338
9.508
1.00
48.46


ATOM
2284
O
SER
A
363
0.830
75.339
10.223
1.00
48.09


ATOM
2285
CB
SER
A
363
−1.226
72.869
9.833
1.00
42.89


ATOM
2286
OG
SER
A
363
−2.557
72.595
9.420
1.00
45.88


ATOM
2287
N
ASP
A
364
1.844
73.597
9.220
1.00
47.51


ATOM
2288
CA
ASP
A
364
3.165
73.949
9.737
1.00
48.11


ATOM
2289
C
ASP
A
364
3.625
75.276
9.160
1.00
53.33


ATOM
2290
O
ASP
A
364
4.274
76.069
9.842
1.00
53.94


ATOM
2291
CB
ASP
A
364
4.191
72.851
9.433
1.00
50.15


ATOM
2292
CG
ASP
A
364
5.086
72.533
10.632
1.00
64.03


ATOM
2293
OD1
ASP
A
364
5.172
73.370
11.557
1.00
65.41


ATOM
2294
OD2
ASP
A
364
5.713
71.449
10.647
1.00
71.20


ATOM
2295
N
ALA
A
365
3.262
75.529
7.908
1.00
49.96


ATOM
2296
CA
ALA
A
365
3.643
76.763
7.230
1.00
50.13


ATOM
2297
C
ALA
A
365
2.702
77.910
7.567
1.00
56.07


ATOM
2298
O
ALA
A
365
2.852
79.027
7.057
1.00
56.87


ATOM
2299
CB
ALA
A
365
3.688
76.546
5.729
1.00
50.69


ATOM
2300
N
GLU
A
366
1.709
77.629
8.393
1.00
52.72


ATOM
2301
CA
GLU
A
366
0.742
78.641
8.767
1.00
52.63


ATOM
2302
C
GLU
A
366
1.186
79.400
10.010
1.00
58.54


ATOM
2303
O
GLU
A
366
1.569
78.800
11.020
1.00
58.58


ATOM
2304
CB
GLU
A
366
−0.631
78.015
8.955
1.00
53.61


ATOM
2305
CG
GLU
A
366
−1.611
78.229
7.855
1.00
57.41


ATOM
2306
CD
GLU
A
366
−2.715
77.189
7.836
1.00
64.87


ATOM
2307
OE1
GLU
A
366
−2.886
76.475
8.858
1.00
51.93


ATOM
2308
OE2
GLU
A
366
−3.400
77.067
6.797
1.00
49.68


ATOM
2309
N
GLU
A
367
1.138
80.720
9.931
1.00
55.76


ATOM
2310
CA
GLU
A
367
1.495
81.554
11.067
1.00
55.95


ATOM
2311
C
GLU
A
367
0.224
81.767
11.870
1.00
58.50


ATOM
2312
O
GLU
A
367
−0.524
82.724
11.624
1.00
58.24


ATOM
2313
CB
GLU
A
367
2.068
82.903
10.594
1.00
57.68


ATOM
2314
CG
GLU
A
367
3.064
82.792
9.423
1.00
69.80


ATOM
2315
CD
GLU
A
367
4.311
81.986
9.778
1.00
93.95


ATOM
2316
OE1
GLU
A
367
4.361
81.402
10.888
1.00
88.27


ATOM
2317
OE2
GLU
A
367
5.249
81.945
8.947
1.00
89.22


ATOM
2318
N
VAL
A
368
−0.052
80.836
12.783
1.00
53.03


ATOM
2319
CA
VAL
A
368
−1.275
80.886
13.574
1.00
51.80


ATOM
2320
C
VAL
A
368
−1.037
81.279
15.029
1.00
52.54


ATOM
2321
O
VAL
A
368
−0.329
80.587
15.765
1.00
51.39


ATOM
2322
CB
VAL
A
368
−2.048
79.541
13.503
1.00
55.79


ATOM
2323
CG1
VAL
A
368
−2.892
79.339
14.742
1.00
55.47


ATOM
2324
CG2
VAL
A
368
−2.914
79.498
12.262
1.00
55.59


ATOM
2325
N
ASP
A
369
−1.641
82.389
15.442
1.00
47.32


ATOM
2326
CA
ASP
A
369
−1.514
82.847
16.816
1.00
46.47


ATOM
2327
C
ASP
A
369
−2.426
82.035
17.727
1.00
49.09


ATOM
2328
O
ASP
A
369
−3.521
82.468
18.071
1.00
47.86


ATOM
2329
CB
ASP
A
369
−1.847
84.330
16.932
1.00
48.19


ATOM
2330
CG
ASP
A
369
−1.569
84.878
18.318
1.00
57.79


ATOM
2331
OD1
ASP
A
369
−0.475
84.606
18.850
1.00
57.84


ATOM
2332
OD2
ASP
A
369
−2.461
85.541
18.891
1.00
64.56


ATOM
2333
N
PHE
A
370
−1.970
80.848
18.100
1.00
42.73


ATOM
2334
CA
PHE
A
370
−2.745
79.965
18.950
1.00
41.31


ATOM
2335
C
PHE
A
370
−3.006
80.575
20.328
1.00
43.47


ATOM
2336
O
PHE
A
370
−4.131
80.550
20.816
1.00
42.61


ATOM
2337
CB
PHE
A
370
−2.061
78.603
19.074
1.00
42.70


ATOM
2338
CG
PHE
A
370
−2.639
77.738
20.148
1.00
44.38


ATOM
2339
CD1
PHE
A
370
−3.909
77.217
20.023
1.00
47.77


ATOM
2340
CD2
PHE
A
370
−1.928
77.477
21.298
1.00
46.49


ATOM
2341
CE1
PHE
A
370
−4.447
76.443
21.017
1.00
48.82


ATOM
2342
CE2
PHE
A
370
−2.462
76.699
22.289
1.00
49.54


ATOM
2343
CZ
PHE
A
370
−3.720
76.180
22.149
1.00
47.81


ATOM
2344
N
ALA
A
371
−1.968
81.133
20.945
1.00
40.03


ATOM
2345
CA
ALA
A
371
−2.100
81.749
22.272
1.00
39.82


ATOM
2346
C
ALA
A
371
−3.124
82.870
22.264
1.00
43.08


ATOM
2347
O
ALA
A
371
−4.018
82.908
23.100
1.00
43.77


ATOM
2348
CB
ALA
A
371
−0.759
82.256
22.768
1.00
40.54


ATOM
2349
N
GLY
A
372
−2.988
83.785
21.315
1.00
38.67


ATOM
2350
CA
GLY
A
372
−3.930
84.891
21.176
1.00
37.87


ATOM
2351
C
GLY
A
372
−5.352
84.337
21.117
1.00
40.50


ATOM
2352
O
GLY
A
372
−6.203
84.695
21.940
1.00
40.40


ATOM
2353
N
TRP
A
373
−5.586
83.418
20.176
1.00
34.91


ATOM
2354
CA
TRP
A
373
−6.897
82.799
20.018
1.00
33.52


ATOM
2355
C
TRP
A
373
−7.354
82.164
21.312
1.00
37.68


ATOM
2356
O
TRP
A
373
−8.466
82.384
21.757
1.00
37.35


ATOM
2357
CB
TRP
A
373
−6.874
81.734
18.917
1.00
31.24


ATOM
2358
CG
TRP
A
373
−8.171
80.954
18.842
1.00
31.42


ATOM
2359
CD1
TRP
A
373
−9.264
81.248
18.068
1.00
34.14


ATOM
2360
CD2
TRP
A
373
−8.527
79.795
19.614
1.00
30.85


ATOM
2361
NE1
TRP
A
373
−10.263
80.329
18.294
1.00
33.31


ATOM
2362
CE2
TRP
A
373
−9.836
79.429
19.238
1.00
34.57


ATOM
2363
CE3
TRP
A
373
−7.857
79.019
20.566
1.00
31.74


ATOM
2364
CZ2
TRP
A
373
−10.489
78.325
19.786
1.00
33.71


ATOM
2365
CZ3
TRP
A
373
−8.508
77.929
21.112
1.00
33.01


ATOM
2366
CH2
TRP
A
373
−9.812
77.594
20.721
1.00
33.65


ATOM
2367
N
LEU
A
374
−6.481
81.361
21.904
1.00
35.27


ATOM
2368
CA
LEU
A
374
−6.787
80.666
23.146
1.00
35.60


ATOM
2369
C
LEU
A
374
−7.196
81.632
24.252
1.00
40.90


ATOM
2370
O
LEU
A
374
−8.235
81.460
24.888
1.00
40.32


ATOM
2371
CB
LEU
A
374
−5.584
79.835
23.600
1.00
35.35


ATOM
2372
CG
LEU
A
374
−5.711
79.184
24.973
1.00
39.66


ATOM
2373
CD1
LEU
A
374
−6.726
78.054
24.916
1.00
39.62


ATOM
2374
CD2
LEU
A
374
−4.357
78.669
25.445
1.00
41.73


ATOM
2375
N
CYS
A
375
−6.373
82.646
24.480
1.00
39.04


ATOM
2376
CA
CYS
A
375
−6.638
83.623
25.537
1.00
39.98


ATOM
2377
C
CYS
A
375
−7.958
84.363
25.398
1.00
43.82


ATOM
2378
O
CYS
A
375
−8.652
84.581
26.385
1.00
42.59


ATOM
2379
CB
CYS
A
375
−5.468
84.584
25.695
1.00
40.64


ATOM
2380
SG
CYS
A
375
−3.964
83.736
26.271
1.00
44.74


ATOM
2381
N
SER
A
376
−8.322
84.722
24.166
1.00
41.18


ATOM
2382
CA
SER
A
376
−9.580
85.432
23.912
1.00
41.32


ATOM
2383
C
SER
A
376
−10.792
84.530
24.112
1.00
46.53


ATOM
2384
O
SER
A
376
−11.872
84.998
24.470
1.00
46.16


ATOM
2385
CB
SER
A
376
−9.607
86.003
22.493
1.00
44.12


ATOM
2386
OG
SER
A
376
−8.321
86.391
22.072
1.00
53.59


ATOM
2387
N
THR
A
377
−10.608
83.238
23.849
1.00
43.48


ATOM
2388
CA
THR
A
377
−11.688
82.265
23.943
1.00
43.03


ATOM
2389
C
THR
A
377
−12.080
81.912
25.367
1.00
46.82


ATOM
2390
O
THR
A
377
−13.265
81.841
25.687
1.00
46.03


ATOM
2391
CB
THR
A
377
−11.348
80.970
23.179
1.00
47.99


ATOM
2392
OG1
THR
A
377
−10.627
81.299
21.997
1.00
47.27


ATOM
2393
CG2
THR
A
377
−12.607
80.234
22.791
1.00
45.64


ATOM
2394
N
ILE
A
378
−11.091
81.640
26.209
1.00
44.34


ATOM
2395
CA
ILE
A
378
−11.375
81.249
27.586
1.00
44.87


ATOM
2396
C
ILE
A
378
−11.280
82.403
28.571
1.00
51.76


ATOM
2397
O
ILE
A
378
−11.265
82.191
29.779
1.00
51.95


ATOM
2398
CB
ILE
A
378
−10.487
80.062
28.059
1.00
47.23


ATOM
2399
CG1
ILE
A
378
−9.028
80.481
28.150
1.00
47.15


ATOM
2400
CG2
ILE
A
378
−10.651
78.861
27.138
1.00
46.98


ATOM
2401
CD1
ILE
A
378
−8.144
79.409
28.713
1.00
50.00


ATOM
2402
N
GLY
A
379
−11.232
83.623
28.046
1.00
50.47


ATOM
2403
CA
GLY
A
379
−11.158
84.822
28.875
1.00
51.42


ATOM
2404
C
GLY
A
379
−9.900
84.845
29.732
1.00
58.97


ATOM
2405
O
GLY
A
379
−9.874
85.464
30.795
1.00
58.13


ATOM
2406
N
LEU
A
380
−8.855
84.178
29.261
1.00
59.15


ATOM
2407
CA
LEU
A
380
−7.598
84.119
29.995
1.00
60.62


ATOM
2408
C
LEU
A
380
−6.996
85.500
30.213
1.00
68.23


ATOM
2409
O
LEU
A
380
−6.925
86.325
29.288
1.00
68.01


ATOM
2410
CB
LEU
A
380
−6.593
83.200
29.296
1.00
60.74


ATOM
2411
CG
LEU
A
380
−6.046
82.052
30.151
1.00
65.43


ATOM
2412
CD1
LEU
A
380
−5.579
80.905
29.281
1.00
65.42


ATOM
2413
CD2
LEU
A
380
−4.918
82.538
31.045
1.00
68.28


ATOM
2414
N
ASN
A
381
−6.566
85.748
31.447
1.00
67.05


ATOM
2415
CA
ASN
A
381
−5.948
87.017
31.817
1.00
67.66


ATOM
2416
C
ASN
A
381
−4.629
86.755
32.543
1.00
72.60


ATOM
2417
O
ASN
A
381
−4.614
86.141
33.616
1.00
72.36


ATOM
2418
CB
ASN
A
381
−6.884
87.822
32.723
1.00
69.06


ATOM
2419
CG
ASN
A
381
−8.084
88.366
31.980
1.00
89.62


ATOM
2420
OD1
ASN
A
381
−7.942
89.116
31.015
1.00
83.72


ATOM
2421
ND2
ASN
A
381
−9.276
87.984
32.423
1.00
80.65


TER
2422

GLN
A
382







ATOM
2423
C01
SCH
Z
1
−2.366
69.257
34.186
1.00
52.86


ATOM
2424
C02
SCH
Z
1
−3.717
69.508
34.220
1.00
50.11


ATOM
2425
N03
SCH
Z
1
−3.848
70.879
34.039
1.00
48.90


ATOM
2426
N04
SCH
Z
1
−2.628
71.508
34.001
1.00
49.93


ATOM
2427
C05
SCH
Z
1
−1.740
70.496
34.107
1.00
51.38


ATOM
2428
N06
SCH
Z
1
−4.780
68.701
34.406
1.00
50.15


ATOM
2429
C07
SCH
Z
1
−5.926
69.153
34.049
1.00
49.91


ATOM
2430
C08
SCH
Z
1
−6.210
70.618
33.803
1.00
49.21


ATOM
2431
C09
SCH
Z
1
−5.130
71.460
33.871
1.00
48.28


ATOM
2432
N10
SCH
Z
1
−5.206
72.835
33.822
1.00
47.03


ATOM
2433
C11
SCH
Z
1
−7.028
68.099
33.875
1.00
49.84


ATOM
2434
C12
SCH
Z
1
−7.413
67.825
32.437
1.00
51.03


ATOM
2435
N13
SCH
Z
1
−8.223
66.605
32.351
1.00
51.54


ATOM
2436
C14
SCH
Z
1
−9.427
66.681
33.191
1.00
50.53


ATOM
2437
C15
SCH
Z
1
−9.096
67.007
34.660
1.00
49.54


ATOM
2438
C16
SCH
Z
1
−8.241
68.265
34.773
1.00
49.61


ATOM
2439
BR17
SCH
Z
1
−1.514
67.591
34.330
1.00
56.51


END

















**************************









The present invention is not to be limited in scope by the specific embodiments described herein. indeed, various modifications of the invention in addition to those described herein will become apparent to those skilled in the art from the foregoing description. Such modifications are intended to fall within the scope of the appended claims.
Patents, patent applications, publications, product descriptions, and protocols are cited throughout this application, the disclosures of which are incorporated herein by reference in their entireties for all purposes.

## Claims

1. An isolated polypeptide comprising the amino acid sequence of SEQ ID NO:1, the amino acid sequence of SEQ ID NO:2, the amino acid sequence of amino acids 25-383 of SEQ ID NO: 1, or the amino acid sequence of amino acids 25-373 of SEQ ID NO:2.

2. The polypeptide of claim 1 comprising the amino acid sequence of SEQ ID NO: 1 or the amino acid sequence of SEQ ID NO: 2.

3. A composition comprising the polypeptide of claim 1.

4. An isolated fusion protein comprising the polypeptide of claim 1 fused to a heterologous protein.